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Université Claude Bernard Lyon I, UFR Chimie-Biochimie UMR CNRS 5013, 69622 Villeurbanne Cedex, France
Correspondence: Address reprint requests to René Buchet, Université Claude Bernard Lyon I, UFR Chimie-Biochimie UMR CNRS 5013, 6 Rue Victor Grignard, 69622 Villeurbanne Cedex, France. Tel.: 33-4-72-43-13-20; Fax: 33-4-72-43-15-43; E-mail: rbuchet{at}univ-lyon1.fr.
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONEXPERIMENTAL PROCEDURESRESULTSDISCUSSIONREFERENCES |
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONEXPERIMENTAL PROCEDURESRESULTSDISCUSSIONREFERENCES |
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; Reid and Wilson, 1971). Sequence comparisons between different AP indicated about 25–30% homology between mammalian AP and Escherichia coli AP (Bradshaw et al., 1981; Kam et al., 1985; Chang et al., 1986; Weiss et al., 1986; Berger et al., 1987; Henthorn et al., 1988; Millán, 1988; Kim and Wyckoff, 1990; Weissig et al., 1993). Four structural genes encoding human AP have been cloned (Kam et al., 1985; Millán, 1986; Henthorn et al., 1987; Millán and Manes, 1988) corresponding to three tissue-specific AP genes located in chromosome 2 (germ-cell, placenta, and intestinal) and one tissue-nonspecific AP gene located in chromosome 1 (Moss, 1992). The mammalian AP, in contrast to the E. coli AP, is a membrane-anchored protein and contains a glycosylphosphatidylinositol anchor linked to the C-terminal carboxyl group of the protein (Low and Finean, 1977; Redman et al., 1994; Ferguson, 1999). Despite differences in their sequences and structures, E. coli AP and mammalian AP catalyze the hydrolysis of almost any phosphomonoester with release of inorganic phosphate and alcohol (Fernley, 1971; Reid and Wilson, 1971). Residues involved in the coordination of two Zn2+ and one Mg2+ ions in the active site and the catalytic serine are preserved from E. coli AP (Kim and Wyckoff, 1990) to human placenta AP (Le Du et al., 2001), whereas most of the surrounding residues are different. This suggests that the mechanisms of catalytic reactions are similar for both enzymes, although mammalian AP are inhibited uncompetitively by L-Phe or L-Arg, whereas E. coli AP are not (Fishman and Sie, 1970,1971; Lin et al., 1971; Byers et al., 1972; Hummer and Millán, 1991; Hoylaerts et al., 1992). During the hydrolysis of phosphate ester by AP, a serine group of AP is phosphorylated. The transient phosphoenzyme is subsequently hydrolyzed to give a noncovalent enzyme-phosphate complex. Under acidic conditions (pH < 6), the hydrolysis of the phosphoenzyme (k3, Scheme 1, taken from Holtz and Kantrowitz, 1999) is rate limiting, whereas dissociation of the noncovalent complex of enzyme with bound phosphate is rate limiting at pH 
8 (k4, Scheme 1) (Chlebowski and Coleman, 1972; Hull et al., 1976; Chlebowski et al., 1977; Gettins and Coleman, 1983). The phosphoenzyme may react with alcohol to form a phosphate ester which dissociates from the enzyme (k5 and k6, Scheme 1).
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; Kozlenkov et al., 2002; Le Du and Millán, 2002). In addition, x-ray observations confirmed the importance of Asp and Glu residues in the catalytic activity of mammalian placental AP. Asp-91 (numbering for the human placental AP), in the vicinity of catalytic Ser-92, is in a hydrogen-bonding distance of Asn-84 (Le Du et al., 2001). Asn-84, Tyr-367, and Glu-429 are probably involved in the allostery (Hoylaerts et al., 1997; Manes et al., 1998; Le Du et al., 2001; Kozlenkov et al., 2002). To probe the mechanisms of hydrolysis by AP, the interaction between vanadate and E. coli AP has been determined by x-ray crystallography (Holtz et al., 1999). Unlike the phosphate ion, vanadate forms five-coordinate complex, mimicking a transition state analog. Comparison between E. coli AP-vanadate complex and the noncovalent E. coli AP-Pi complex indicates that active site residues moved only slightly (Holtz et al., 1999). The x-ray structure of mammalian placental AP (Le Du et al., 2001), shows that the amino acid residues in the active site are preserved as compared with the x-ray structure of E. coli AP. The conformational changes of mammalian AP induced by Pi binding in water medium were not reported. Based on the similarity of the active site in E. coli AP and mammalian AP, one would expect that Pi binding in mammalian AP would induce similar conformational effects than in E. coli AP. Due to the electrostatic interactions between phosphate groups and charged side chain residues, water molecules may play a role in mediating such interactions.
In this work, we investigated the structural changes of mammalian AP in water medium caused by ligand binding in the active site, by using reaction-induced infrared difference spectroscopy (RIDS). RIDS cannot provide a detailed structure of the whole protein as x-ray data do. However, RIDS allows us to measure very small deviations at a single vibrational group, caused by the effects of substrate bindings in the active site of enzymes in water medium (Mäntele, 1993; Siebert, 1995; Cepus et al., 1998; Zscherp and Barth, 2001; Barth and Zscherp, 2002). By taking advantage of the knowledge of the resolved 3D structure of the whole mammalian AP and by measuring small fluctuations of structure changes, we can provide specific details on the deviation of structural changes, such as the magnitude of structural changes (approximate number of amino acids implicated in the ligand binding) as well the changes in hydrogen bond strengths affecting peptide backbone and side chain residues.
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EXPERIMENTAL PROCEDURES |
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TOPABSTRACTINTRODUCTIONEXPERIMENTAL PROCEDURESRESULTSDISCUSSIONREFERENCES |
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Infrared spectra of samples in 2H2O buffer
Purified IAP (10 mg/ml corresponding to 0.09 mM assuming a 114-KDa dimeric enzyme) were dissolved either in buffer A or in buffer B. 2H2O buffer A contained 100 mM Tris-HCl, p2H = 7.0, 10 mM MgCl2 and 2.5–10 mM NPE-caged ATP with or without 5 mM adenosine. 2H2O buffer B contained 100 mM phosphate, p2H = 7.0, 10 mM MgCl2 and 4–8 mM NPE-caged ATP with or without 5 mM adenosine. Control samples without protein were prepared under the same conditions. The p2H was measured with a glass electrode and was corrected by a value of 0.4 (p2H 7.0 = pH 7.4, Glasoe and Long, 1960). Freshly prepared samples were loaded between two circular CaF2 windows separated by a 50 µm thick Teflon spacer. They were incubated for 10 min in the dark, before infrared measurements. The infrared cell was thermostated at 20°C with a circulating bath. The optical resolution was 4 cm–1 but spectral points were encoded every 2 cm–1. Collected were 256 scans during about 4 min, coadded and Fourier transformed. Then the sample was illuminated for 120 s by means of a 150 W xenon lamp (without filter) to induce complete photorelease of substrates from their cage. The reaction-induced infrared difference spectra (RIDS) of the sample were obtained by subtracting the spectrum measured before illumination from the spectrum measured after the illumination. Five sets of RIDS corresponding to samples in buffer A, whereas three sets of RIDS corresponding to samples in buffer B were measured and coadded to obtain a better signal/noise ratio. The final RIDS were corrected for water-vapor absorption according to Goormaghtigh et al., 1994.
Infrared spectra of samples in H2O buffer
Purified IAP (50 mg/ml corresponding to 0.45 mM assuming a 114-KDa dimeric enzyme) was prepared in H2O buffer, containing 200 mM Tris-HCl, pH = 7.4, 10 mM MgCl2 and 20 mM NPE-caged ATP. The same buffer without IAP was used as a control. Freshly prepared samples were loaded between two circular CaF2 windows separated by a 6 µm thick Teflon spacer. The RIDS were determined under the same conditions as described above. Three sets of RIDS were measured and coadded to obtain a better signal/noise ratio.
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RESULTS |
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TOPABSTRACTINTRODUCTIONEXPERIMENTAL PROCEDURESRESULTSDISCUSSIONREFERENCES |
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), the released ATP is hydrolyzed mostly by a stepwise production of three Pi by forming sequentially ADP, AMP, and adenosine (Fig. 1). However, NPE-caged ATP can be hydrolyzed before the photolysis due to the very low activity of phosphodiesterase of IAP (O'Brien and Herschlag, 2001), especially in the case of relatively high concentration of IAP.
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). The pH of the solution was set at 7.4, which has the advantage to slow down the activity of IAP by a factor of about 35 times as compared with the pH set at 10.5 (Sarrouilhe et al., 1993), whereas the secondary structure of IAP is preserved over the pH range from 7.4 to 10.5 (de La Fournière et al., 1995). The overall infrared spectrum of IAP in the amide-I and amide-II regions was identical to that of IAP previously reported (de La Fournière et al., 1995; Bortolato et al., 1999). UV illumination of IAP without NPE-caged ATP did not produce any infrared changes (results not shown), thus indicating that UV illumination did not affect the secondary structure of IAP. Photoconversion of NPE-caged ATP without protein in Tris-HCl buffer (trace i of Fig. 2), induced in the infrared spectrum, two negative bands located at 1527–1530 cm–1 and at 1346–1348 cm–1 (signaling the disappearance of the nitro group) and a positive band located at 1688–1684 cm–1 (indicating the formation of a carbonyl group) (Barth et al., 1990, 1997). The RIDS of NPE-caged ATP with IAP in Tris-HCl buffer (trace ii of Fig. 2) is dominated by the photo conversion of NPE-caged ATP. However, small but reproducible changes were observed in the difference spectra (trace iii of Fig. 2), corresponding to spectrum ii minus spectrum i. The 1685–1688 cm–1, 1527–1530 cm–1, and 1346–1348 cm–1 bands associated to the photo conversion of NPE-caged ATP were used to normalize the contributions from the photolytic release of the NPE-caged nucleotide between samples (Barth et al., 1991; Cepus et al., 1998; Butler et al., 2002). The difference infrared spectra should reflect structural changes caused by binding of Pi, adenosine, or 2-nitrosoacetophenone, since infrared spectra were measured before and 5 min after photolysis to ensure complete hydrolysis of ATP by IAP. The structural alterations observed in the 1800–1300 cm–1 region (trace iii of Fig. 2) were accompanied by changes in phosphate vibra-tions (Fig. 3). As reported (Barth et al., 1990, 1997; Cepus et al., 1998), the photolysis of NPE-caged GTP or NPE-caged ATP in the absence of protein induced a positive band at 1124–1120 cm–1 as well as two negative bands at 1078 cm–1 and 1060 cm–1 (trace i of Fig. 3) indicative of the release of nucleotide from its cage. Photolysis of NPE-caged ATP in the presence of IAP (trace ii of Fig. 3) induced changes of phosphate groups caused by the catalytic activity of IAP, indicating complete hydrolysis of ATP. There was no time dependence of the infrared changes after 2 min photolysis and after 5 min collecting the infrared spectra. The magnitude of structural changes of IAP was assessed by determining the ratio of intensities of amide-1 band of IAP in the presence of NPE-caged ATP before photolysis (spectrum i in Fig. 4) and its corresponding amide-I change in the RIDS of IAP in the presence of NPE-caged ATP (spectrum ii in Fig. 4). The COBSI index (Barth et al., 1996), which is the ratio of intensities 
A/2A, was 0.0085. This value corresponded to 2 amino acids per monomeric IAP, involved in the structural changes of IAP caused by the binding of Pi, adenosine, or photoproduct.
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; Venyaminov and Kalnin, 1990; Goormaghtigh et al., 1994a,b; Barth, 2000). The intensities of the 1639 cm–1, 1631 cm–1, and 1576 cm–1 negative peaks, as well as the 1622 cm–1 and 1585 cm–1 positive peaks, increased by two- to threefold with increasing concentrations of NPE-caged ATP from 2.5 mM to 10 mM (Fig. 7). The increase of the initial NPE-caged ATP concentration and the low IAP concentration could contribute both to the increase of nonhydrolyzed NPE-caged ATP, before the photolysis. Under these conditions the phosphomonoesterase activity can be monitored. Furthermore, the inorganic phosphate is a competitive inhibitor of IAP with Ki = 1.86 ± 0.1 mM (determined in this work under the same conditions as for IR samples), inferring that the structural changes could not have been solely promoted by the interactions of Pi with IAP. Indeed, a partial saturation of Pi binding would have been observed, since after complete ATP hydrolysis, three inorganic phosphates were released from 2.5–10 mM NPE-caged ATP, leading to 80–94% saturation of Pi binding site of IAP.
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First, a 100 mM phosphate buffer p2H 7.0 was used instead of 100 mM Tris-HCl buffer p2H 7.0, to saturate the Pi binding site of IAP. The RIDS of NPE-caged ATP with IAP in 100 mM Tris-HCl buffer p2H 7.0 and 10 mM Mg2+ (Fig. 8 A) was slightly different from that of NPE-caged ATP with IAP in 100 mM phosphate buffer p2H 7.0 and 10 mM Mg2+ (Fig. 8 B). Four positive peaks located at 1671 cm–1, 1655–1658 cm–1, 1622–1623 cm–1, and 1596 cm–1, 1585 cm–1 remained unaffected during the change of buffer, suggesting that they are not due to the interactions between inorganic phosphate and IAP. The intensities of the negative peaks located around 1631 cm–1 and 1639 cm–1 decreased in intensity when the Tris-HCl buffer was changed for the phosphate buffer.
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Thirdly, RIDS of 0.09 mM IAP in Tris-HCl buffer p2H 7.0 containing 5 mM NPE-caged ATP, 10 mM Mg2+, and 50 mM L-Phe (an uncompetitive inhibitor of IAP as well as a derivative of 2-nitrosoacetophenone) was identical to the RIDS of IAP under the same conditions but without L-Phe (results not shown). This indicates that the uncompetitive site of IAP was not involved in the structural changes. The infrared changes observed at 1631 cm–1 and 1639 cm–1 could indicate interactions between phosphate groups with IAP although other interpretations cannot be excluded. The peaks located at 1670–1671 cm–1, 1651–1658 cm–1, and 1596 cm–1 may signal interactions between IAP with 2-nitrosoacetophenone.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONEXPERIMENTAL PROCEDURESRESULTSDISCUSSIONREFERENCES |
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; Siebert, 1995; Cepus et al., 1998; Zscherp and Barth, 2001; Barth and Zscherp, 2002). NPE-caged ATP was selected as alkaline phosphatase substrate since it is commercially available and it is conveniently used to monitor structural changes caused by nucleotide binding (Troullier et al., 1996; Raimbault et al., 1997; Von Germar et al., 1999; Geibel et al., 2000; Allin and Gerwert, 2001; Granjon et al., 2001; Butler et al., 2002; Kirilenko et al., 2002; Liu and Barth, 2003).
Structural changes related to phosphate-binding induced changes in the active site
The overall infrared changes that were observed in the amide-I region, after photorelease and complete hydrolysis of 5 mM ATP by mammalian IAP in aqueous solution, corresponded to the involvement of 2 amino acid residues per monomer IAP, based on the ratio of infrared intensities as determined by COBSI index. This index is a measure of change of backbone structure and interactions and may underestimate the number of amino acid residues affected, due to band overlapping (Barth et al., 1996; Scheirlinckx et al., 2001). We cannot neglect the phosphodiesterase activity of IAP, before the photorelease of ATP from the NPE-caged ATP, especially when the IAP concentration was high (0.45 mM dimeric IAP in H2O Tris-HCl buffer), contributing to underestimation of the number of amino acid residues affected. The phosphodiesterase activity, although very small (it is about 106 times lower than the monophosphoesterase activity) was clearly assigned to E. coli alkaline phosphatase and not to any phosphodiesterase contaminant (O'Brien and Herschlag, 2002). Therefore, to better observe the structural changes caused by the phosphate binding, it was necessary to decrease IAP concentration (down to 0.09 mM) and to increase the NPE-caged ATP (from 2mM to 10 mM). The comparison of the RIDS of IAP in 100 mM Tris-HCl buffer pH 7.4, favoring the formation of a Tris-phosphate complex and its dissociation (k5 and k6, Scheme 1) (Trentham and Gutfreund, 1968) or in 100 mM phosphate buffer (saturating the active site with Pi) allowed us to identify putative infrared changes associated with phosphate groups. These changes consisted in a decrease in intensities of the infrared bands located at 1631 cm–1 and at 1639 cm–1, suggesting a very small distortion of the peptide carbonyl backbone. Based on the relative ratio of infrared intensities, these changes corresponded to less than one amino acid residue. Whether the changes in the intensities of the two bands are solely related to the interactions of phosphate groups with IAP remains to be further investigated. Nevertheless, these results indicate that the difference between IAP and IAP-Pi complex in water medium involved only very small structural changes. Recently, x-ray diffraction data indicated that 
was bound in the active site of E. coli AP, providing a structural model for the transition state in the enzyme catalyzed reaction (Holtz et al., 1999). Comparison between E. coli AP-vanadate complex and E. coli AP-Pi complex shows that the active site residues move only slightly to accommodate the transition state (Holtz et al., 1999). Our work indicates that Pi binding induced only minimal structural changes for the mammalian IAP, in accordance with the x-ray results on E. coli AP. In addition, RIDS did not reveal that water molecules could affect the conformational changes induced by Pi-binding. Although water molecules may surround the charged Pi groups, it appears that the binding of Pi to IAP in aqueous medium had no additional structural effects on IAP. This tends to suggest that Pi or vanadate binding involve only elastic collisions and is consistent with alkaline phosphatase being a "perfect enzyme" at pH range from 7 to 8 (Simopoulos and Jencks, 1994; O'Brien and Herschlag, 2001,2002), where kcat/Km (as determined for the E. coli enzyme) is maximum. The mechanism of Pi inhibition is probably not associated with conformational changes but Pi may serve passively to hinder the active site.
Structural changes due to the interaction of 2-nitrosoacetophenone with alkaline phosphatase
The photolysis of NPE-caged ATP produced 2-nitrosoaceto-phenone (free cage) and ATP, which was sequentially hydrolyzed by IAP giving rise to adenosine and three Pi. Since only a part of the RIDS could be assigned to the conformational changes induced by the interactions of Pi with IAP, the remaining part could be related to the interactions of adenosine, 2-nitrosoacetophenone or NPE-caged ATP with IAP. Indeed, saturation of Pi, interacting with the active site, did not completely hinder the infrared changes, thus indicating that Pi binding could not have induced all the infrared changes. Addition of 5 mM of adenosine did not prevent the infrared changes, suggesting that adenosine did not interact with IAP. Therefore, it was concluded that NPE-caged ATP or 2-nitrosoacetophenone could induce structural changes at 1670–1671 cm–1, 1651–1658 cm–1, and 1596 cm–1, affecting at least one or two amino acid residues of the peptide backbone when considering the ratio of infrared intensities in the amide-I region. The location of the binding site of 2-nitrosoacetophenone with IAP is outside of the active site of IAP and the uncompetitive binding site of L-Phe in IAP, since the addition of 100 mM phosphate or 50 mM L-Phe in IAP samples could not prevent completely the infrared changes of the protein in the amide-I region.
Submitted on September 2, 2003; accepted for publication February 23, 2004.
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REFERENCES |
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TOPABSTRACTINTRODUCTIONEXPERIMENTAL PROCEDURESRESULTSDISCUSSIONREFERENCES |
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Barth, A. 2000. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol. 74:141–173.[CrossRef][Medline]
Barth, A., J. T. E. Corie, M. J. Gradwell, Y. Maeda, W. Mäntele, T. Meier, and D. R. Trentham. 1997. Time-resolved infrared spectroscopy of intermediates and products from photolysis of 1-(2-Nitrophenyl)ethyl phosphates: Reaction of the 2-Nitrosoacetophenone byproducts with thiols. J. Am. Chem. Soc. 119:4149–4159.[CrossRef]
Barth, A., W. Kreutz, and W. Mäntele. 1990. Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity. A Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle. FEBS Lett. 277:147–150.[CrossRef][Medline]
Barth, A., W. Mäntele, and W. Kreutz. 1991. Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase. Biochim. Biophys. Acta. 1057:115–123.[Medline]
Barth, A., F. Von Germar, W. Kreutz, and W. Mäntele. 1996. Time-resolved infrared spectroscopy of the Ca2+-ATPase. The enzyme at work. J. Biol. Chem. 271:30637–30646.
Barth, A., and C. Zscherp. 2002. What vibrations tell us about proteins. Q. Rev. Biophys. 35:369–430.[CrossRef][Medline]
Butler, B. C., R. H. Hanchett, H. Rafailov, and G. MacDonald. 2002. Investigating structural changes induced by nucleotide binding to RecA using difference FTIR. Biophys. J. 82:2198–2210.
Berger, J., E. Garattini, J.-C. Hua, and S. Udenfriend. 1987. Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc. Natl. Acad. Sci. USA. 84:695–698.
Bortolato, M., Besson, F., and Roux, B. 1999. An infrared study of the thermal and pH stabilities of the GPI-alkaline phosphatase from bovine intestine. Proteins. 37: 310–318.[CrossRef][Medline]
Bradshaw, R. A., F. Cancedda, L. H. Ericsson, P. A. Newman, S. P. Piccoli, M. J. Schlessinger, K. Shriefer, and K. A. Walsh. 1981. Amino acid sequence of Escherichia coli alkaline phosphatase. Proc. Natl. Acad. Sci. USA. 78:3473–3477.
Butler, B. C., R. H. Hanchett, H. Rafailov, and G. MacDonald. 2002. Investigating structural changes induced by nucleotide binding to RecA using difference FTIR. Biophys. J. 82:2198–2210.
Byers, D. A., H. N. Fernley, and P. G. Walker. 1972. Studies on alkaline phosphatase. Inhibition of human-placental phosphoryl phosphatase by L-phenylalanine. Eur. J. Biochem. 29:197–204.[Medline]
Cepus, V., C. Ulbrich, C. Allin, A. Trouiller, and K. Gerwert. 1998. Fourier transform infrared photolysis studies of caged compounds. Methods Enzymol. 291:223–245.[Medline]
Chang, C. N., W.-J. Kuang, and E. Y. Cheng. 1986. Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. Gene. 44:121–125.[CrossRef][Medline]
Chirgadze, Y. N., O. V. Fedorov, and N. P. Trushina. 1975. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers. 14:679–694.[CrossRef][Medline]
Chlebowski, J. F., I. M. Armitage, and J. E. Coleman. 1977. Allosteric interactions between metal ion and phosphate at the active sites of alkaline phosphatase as determined by 31P NMR and 113Cd NMR. J. Biol. Chem. 252:7053–7061.
Chlebowski, J. F., and J. E. Coleman. 1972. Presteady state kinetics of phosphorothioate hydrolysis by alkaline phosphatase. J. Biol. Chem. 247:6007–6010.
de La Fournière, L., O. Nosjean, R. Buchet, and B. Roux. 1995. Thermal and pH stabilities of alkaline phosphatase from bovine intestinal mucosa: a FTIR study. Biochim. Biophys. Acta. 1248:186–192.[CrossRef][Medline]
Fernley, H. N. 1971. Mammalian alkaline phosphatase. In The Enzymes, 3rd ed. P. D. Boyer, editor. Academic Press, New York and London. 417–447.
Ferguson, M. A. J. 1999. The structure, biosynthesis and functions of glycosyl-phosphatidylinositol anchors, and the contributions of trypanosome research. J. Cell Sci. 112:2799–2809.[Abstract]
Fishman, W., and H. G. Sie. 1970. L-homoarginine; an inhibitor of serum "bone and liver" alkaline phosphatase. Clin. Chim. Acta. 29:339–341.[CrossRef][Medline]
Fishman, W. H., and H. G. Sie. 1971. Organ-specific inhibition of human alkaline phosphatase isoenzymes of liver, bone, intestine and placenta; L-phenylalanine, L-tryptophan and L-homoarginine. Enzymologia. 41:141–167.[Medline]
Geibel, S., A. Barth, S. Amslinger, A. H. Jung, C. Burzik, R. J. Clarke, R. S. Givens, and K. Fendler. 2000. P(3)-[2-(4-hydroxyphenyl)-2-oxo]ethyl ATP for the rapid activation of the Na(+), K(+)-ATPase. Biophys. J. 79:1346–1357.
Gettins, P., and J. E. Coleman. 1983. 31P nuclear magnetic resonance of phospho-enzyme intermediates of alkaline phosphatase. J. Biol. Chem. 258:408–416.
Glasoe, P. K., and F. A. Long. 1960. Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 64:188–190.[CrossRef]
Goormaghtigh, E., V. Cabiaux, and J.-M. Ruysschaert. 1994a. Subtraction of atmospheric water contribution in Fourier transform infrared spectroscopy of biological membranes and proteins. Spectrochim. Acta, Part A. 51A:2137–2144.[CrossRef]
Goormaghtigh, E., V. Cabiaux, and J.-M. Ruysschaert. 1994b. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange. Subcell. Biochem. 23:363–403.[Medline]
Granjon, T., M.-J. Vacheron, C. Vial, and R. Buchet. 2001. Structural changes of mitochondrial creatine kinase upon binding of ADP, ATP, or Pi, observed by reaction-induced infrared difference spectra. Biochemistry. 40:2988–2994.[CrossRef][Medline]
Henthorn, P. S., M. Raducha, Y. H. Edwards, M. J. Weiss, C. Slaughter, M. A. Lafferty, and H. Harris. 1987. Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc. Natl. Acad. Sci. USA. 84:1234–1238.
Henthorn, P. S., M. Raducha, T. Kadesch, M. J. Weiss, and H. Harris. 1988. Structure of the human liver/bone/kidney alkaline phosphatase gene. J. Biol. Chem. 263:12011–12019.
Holtz, K. M., and E. R. Kantrowitz. 1999. The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis. FEBS Lett. 462:7–11.[CrossRef][Medline]
Holtz, K. M., B. Stec, and E. R. Kantrowitz. 1999. A model of the transition state in the alkaline phosphatase reaction. J. Biol. Chem. 274:8351–8354.
Hoylaerts, M. F., T. Manes, and J. L. Millán. 1992. Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase. Biochem. J. 286:23–30.[Medline]
Hoylaerts, M. F., T. Manes, and J. L. Millán. 1997. Mammalian alkaline phosphatases are allosteric enzymes. J. Biol. Chem. 272:22781–22787.
Hull, W. E., S. E. Halford, H. Gutfreund, and B. D. Sykes. 1976. 31P nuclear magnetic resonance study of alkaline phosphatase: The role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pH. Biochemistry. 15:1547–1561.[CrossRef][Medline]
Hummer, G., and J. L. Millán. 1991. Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by L-leucine. Biochem. J. 274:91–95.[Medline]
Kam, W., E. Clauser, Y. S. Kim, Y. W. Kan, and W. Rutter. 1985. Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc. Natl. Acad. Sci. USA. 82:8715–8719.
Kim, E. E., and H. W. Wyckoff. 1990. Structure of alkaline phosphatases. Clin. Chim. Acta. 186:175–188.[CrossRef][Medline]
Kim, E. E., and H. W. Wyckoff. 1991. Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J. Mol. Biol. 218:449–464.[CrossRef][Medline]
Kirilenko, A., M. Golczak, S. Pikula, R. Buchet, and J. Bandorowicz-Pikula. 2002. GTP-induced membrane binding and ion channel activity of annexin VI: is annexin VI a GTP biosensor? Biophys. J. 82:2737–2745.
Kozlenkov, A., T. Manes, M. F. Hoylaerts, and J. L. Millan. 2002. Function assignment to conserved residues in mammalian alkaline phosphatases. J. Biol. Chem. 277:22992–22999.
Le Du, M.-H., and J.-L. Millán. 2002. Structural evidence of functional divergence in human alkaline phosphatases. J. Biol. Chem. 277:49808–49814.
Le Du, M.-H., T. Stigbrand, M. J. Tausig, A. Ménez, and E. A. Stura. 2001. Crystal structure of alkaline phosphatase from human placenta at 1.8 Â resolution. Implication for a substrate specificity. J. Biol. Chem. 276:9158–9165.
Lin, C. W., H. G. Sie, and W. H. Fishman. 1971. L-tryptophan. A non-allosteric organ-specific uncompetitive inhibitor of human placental alkaline phosphatase. Biochem. J. 124:509–516.[Medline]
Liu, M., and A. Barth. 2003. Mapping interactions between the Ca2+ ATPase and its substrate ATP with infrared spectroscopy. J. Biol. Chem. 278:10112–10118.
Low, M. G., and J. B. Finean. 1977. Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C. Biochem. J. 167:281–284.[Medline]
Manes, T., M. F. Hoylaerts, R. Müller, F. Lottspeich, W. Hölke, and J. L. Millán. 1998. Genetic complexity, structure, and characterization of highly active bovine intestinal alkaline phosphatases. J. Biol. Chem. 273:23353–23360.
Mäntele, W. 1993. Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms. Trends Biochem. Sci. 18:197–202.[CrossRef][Medline]
Millán, J.-L. 1986. Molecular cloning and sequence analysis of human placental alkaline phosphatase. J. Biol. Chem. 261:3112–3115.
Millán, J.-L. 1988. Oncodevelopmental expression and structure of alkaline phosphatase genes. Anticancer Res. 8:995–1004.[Medline]
Millán, J.-L., and T. Manes. 1988. Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc. Natl. Acad. Sci. USA. 85:3024–3028.
Moss, D. W. 1992. Perspectives in alkaline phosphatase research. Clin. Chem. 38:2486–2492.
O'Brien, P. J., and D. Herschlag. 2001. Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatases. Biochemistry. 40:5691–5699.[CrossRef][Medline]
O'Brien, P. J., and D. Herschlag. 2002. Alkaline phosphatase revisited: hydrolysis of alkyl phosphates. Biochemistry. 41:3207–3225.[CrossRef][Medline]
Raimbault, C., F. Besson, and R. Buchet. 1997. Conformational changes of arginine kinase induced by photochemical release of nucleotides from caged nucleotides: an infrared difference-spectroscopy investigation. Eur. J. Biochem. 244:343–351.[Medline]
Redman, C. A., J. E. Thomas-Oates, S. Ogata, Y. Ikehara, and M. A. Ferguson. 1994. Structure of the glycosylphosphatidylinositol membrane anchor of human placental alkaline phosphatase. Biochem. J. 302:861–865.[Medline]
Reid, T. W., and I. B. Wilson. 1971. E. coli alkaline phosphatase. In The Enzymes, 3rd ed. P. D. Boyer, editor. Academic Press, New York and London. 373–415.
Sarrouilhe, D., P. Lalegerie, and M. Baudry. 1993. Alkaline phosphatase activity at physiological pH: kinetic properties and biological significance. Cell. Mol. Biol. 39:13–19.[Medline]
Scheirlinckx, F., R. Buchet, J.-M. Ruysschaert, and E. Goormaghtigh. 2001. Monitoring of secondary and tertiary structure changes in the gastric H+/K+-ATPase by infrared spectroscopy. Eur. J. Biochem. 268:3644–3653.[Medline]
Siebert, F. 1995. Infrared spectroscopy applied to biochemical and biological problems. Methods Enzymol. 246:501–526.[Medline]
Simopoulos, T. T., and W. P. Jencks. 1994. Alkaline phosphatase is an almost perfect enzyme. Biochemistry. 33:10375–10380.[CrossRef][Medline]
Trentham, D. R., and H. Gutfreund. 1968. The kinetics of the reaction of nitrophenyl phosphates with alkaline phosphatase from Escherichia coli. Biochem. J. 106:455–460.[Medline]
Troullier, A., K. Gerwert, and Y. Dupont. 1996. A time-resolved Fourier transformed infrared difference spectroscopy study of the sarcoplasmic reticulum Ca(2+)-ATPase: kinetics of the high-affinity calcium binding at low temperature. Biophys. J. 71:2970–2983.
Venyaminov, S. Y., and N. N. Kalnin. 1990. Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers. 30:1243–1257.[CrossRef][Medline]
Von Germar, F., A. Galan, O. Llorca, J. L. Carrascoa, J. M. Valpuesta, W. Mäntele, and A. Muga. 1999. Conformational changes generated in GroEL during ATP hydrolysis as seen by time-resolved infrared spectroscopy. J. Biol. Chem. 274:5508–5513.
Weiss, M. J., P. S. Henthorn, M. A. Lafferty, C. Slaughter, M. Raducha, and H. Harris. 1986. Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc. Natl. Acad. Sci. USA. 83:7182–7186.
Weissig, H., A. Schildge, M. F. Hoylaerts, M. Iqbal, and J. L. Millán. 1993. Cloning and expression of the bovine intestinal alkaline phosphatase gene: biochemical characterization of the recombinant enzyme. Biochem. J. 290:503–508.[Medline]
Zscherp, C., and A. Barth. 2001. Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms. Biochemistry. 40:1875–1883.[CrossRef][Medline]
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