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Items: 1 to 20 of 41

1.
Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli
Rageia Elfageih, Alexandros Karyolaimos, Grant Kemp, Jan‐Willem de Gier, Gunnar von Heijne, Renuka Kudva
Protein Sci. 2020 Oct; 29(10): 2028–2037. Published online 2020 Aug 24. doi: 10.1002/pro.3927
PMCID:
PMC7513700
AbstractArticlePDF–2.2M
2.
Kinetic Isotope Effects for Alkaline Phosphatase Reactions: Implications for the Role of Active Site Metal Ions in Catalysis
Jesse G. Zalatan, Irina Catrina, Rebecca Mitchell, Piotr K. Grzyska, Patrick J. O’Brien, Daniel Herschlag, Alvan C. Hengge
J Am Chem Soc. Author manuscript; available in PMC 2011 Sep 12.
Published in final edited form as: J Am Chem Soc. 2007 Aug 8; 129(31): 9789–9798. Published online 2007 Jul 14. doi: 10.1021/ja072196+
PMCID:
PMC3171187
AbstractArticlePDF–1.4M
3.
Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases
Dimitris Koutsioulis, Andrzej Lyskowski, Seija Mäki, Ellen Guthrie, Georges Feller, Vassilis Bouriotis, Pirkko Heikinheimo
Protein Sci. 2010 Jan; 19(1): 75–84. Published online 2009 Nov 13. doi: 10.1002/pro.284
PMCID:
PMC2817841
AbstractArticlePDF–286K
4.
Comparative Enzymology in the Alkaline Phosphatase Superfamily to Determine the Catalytic Role of an Active Site Metal Ion
Jesse G. Zalatan, Timothy D. Fenn, Daniel Herschlag
J Mol Biol. Author manuscript; available in PMC 2009 Dec 31.
Published in final edited form as: J Mol Biol. 2008 Dec 31; 384(5): 1174–1189. Published online 2008 Oct 2. doi: 10.1016/j.jmb.2008.09.059
PMCID:
PMC2622731
AbstractArticlePDF–2.3M
5.
Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of Arg166 Mutations in Escherichia coli Alkaline Phosphatase
Patrick J. O'Brien, Jonathan Kyle Lassila, Timothy D. Fenn, Jesse G. Zalatan, Daniel Herschlag
Biochemistry. Author manuscript; available in PMC 2009 Jul 22.
Published in final edited form as: Biochemistry. 2008 Jul 22; 47(29): 7663–7672. doi: 10.1021/bi800545n
PMCID:
PMC2587100
AbstractArticlePDF–1.1M
6.
Alkaline Phosphatase Mono- and Di-esterase Reactions: Comparative Transition State Analysis
Jesse G. Zalatan, Daniel Herschlag
J Am Chem Soc. Author manuscript; available in PMC 2008 Sep 17.
Published in final edited form as: J Am Chem Soc. 2006 Feb 1; 128(4): 1293–1303. doi: 10.1021/ja056528r
PMCID:
PMC2538955
AbstractArticlePDF–921K
7.
Probing the Origin of the Compromised Catalysis of E. coli Alkaline Phosphatase in its Promiscuous Sulfatase Reaction
Irina Catrina, Patrick J. O'Brien, Jamie Purcell, Ivana Nikolic-Hughes, Jesse G. Zalatan, Alvan C. Hengge, Daniel Herschlag
J Am Chem Soc. Author manuscript; available in PMC 2008 Sep 8.
Published in final edited form as: J Am Chem Soc. 2007 May 2; 129(17): 5760–5765. Published online 2007 Apr 6. doi: 10.1021/ja069111+
PMCID:
PMC2532492
AbstractArticlePDF–508K
8.
Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine
Jie Wang, Evan R. Kantrowitz
Protein Sci. 2006 Oct; 15(10): 2395–2401. doi: 10.1110/ps.062351506
PMCID:
PMC2242381
AbstractArticlePDF–298K
9.
Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes.
K. M. Holtz, B. Stec, J. K. Myers, S. M. Antonelli, T. S. Widlanski, E. R. Kantrowitz
Protein Sci. 2000 May; 9(5): 907–915. doi: 10.1110/ps.9.5.907
PMCID:
PMC2144633
SummaryPDF–1.1M
10.
Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites.
L. Ma, T. T. Tibbitts, E. R. Kantrowitz
Protein Sci. 1995 Aug; 4(8): 1498–1506. doi: 10.1002/pro.5560040807
PMCID:
PMC2143176
SummaryPDF–1.6M
11.
A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase
Kechao Yang, William W. Metcalf
Proc Natl Acad Sci U S A. 2004 May 25; 101(21): 7919–7924. Published online 2004 May 17. doi: 10.1073/pnas.0400664101
PMCID:
PMC419532
AbstractArticlePDF–439K
12.
Amino acid sequence of Escherichia coli alkaline phosphatase.
R A Bradshaw, F Cancedda, L H Ericsson, P A Neumann, S P Piccoli, M J Schlesinger, K Shriefer, K A Walsh
Proc Natl Acad Sci U S A. 1981 Jun; 78(6): 3473–3477. doi: 10.1073/pnas.78.6.3473
PMCID:
PMC319591
SummaryPage BrowsePDF–727K
13.
Sequence of the gene for alkaline phosphatase from Escherichia coli JM83.
H Shuttleworth, J Taylor, N Minton
Nucleic Acids Res. 1986 Nov 11; 14(21): 8689. doi: 10.1093/nar/14.21.8689
PMCID:
PMC311889
SummaryPage BrowsePDF–103K
14.
Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli.
R F DuBose, D E Dykhuizen, D L Hartl
Proc Natl Acad Sci U S A. 1988 Sep; 85(18): 7036–7040. doi: 10.1073/pnas.85.18.7036
PMCID:
PMC282115
SummaryPage BrowsePDF–1.1M
15.
New pleiotropic alkaline phosphatase-negative mutants of Escherichia coli K-12.
M Heyde, R Portalier
J Bacteriol. 1982 Aug; 151(2): 529–533. doi: 10.1128/jb.151.2.529-533.1982
PMCID:
PMC220292
SummaryPage BrowsePDF–701K
16.
Use of gene fusions to determine the orientation of gene phoA on the Escherichia coli chromosome.
A Sarthy, S Michaelis, J Beckwith
J Bacteriol. 1981 Jan; 145(1): 293–298. doi: 10.1128/jb.145.1.293-298.1981
PMCID:
PMC217272
SummaryPage BrowsePDF–982K
17.
Deletion map of the Escherichia coli structural gene for alkaline phosphatase, phoA.
A Sarthy, S Michaelis, J Beckwith
J Bacteriol. 1981 Jan; 145(1): 288–292. doi: 10.1128/jb.145.1.288-292.1981
PMCID:
PMC217271
SummaryPage BrowsePDF–711K
18.
Cloning and restriction mapping of the alkaline phosphatase structural gene (phoA) of Escherichia coli and generation of deletion mutants in vitro.
H Inouye, S Michaelis, A Wright, J Beckwith
J Bacteriol. 1981 May; 146(2): 668–675. doi: 10.1128/jb.146.2.668-675.1981
PMCID:
PMC217011
SummaryPage BrowsePDF–1.1M
19.
Cloning and characterization of the Escherichia coli gene coding for alkaline phosphatase.
P E Berg
J Bacteriol. 1981 May; 146(2): 660–667. doi: 10.1128/jb.146.2.660-667.1981
PMCID:
PMC217010
SummaryPage BrowsePDF–1.2M
20.
Signal sequence of alkaline phosphatase of Escherichia coli.
H Inouye, W Barnes, J Beckwith
J Bacteriol. 1982 Feb; 149(2): 434–439. doi: 10.1128/jb.149.2.434-439.1982
PMCID:
PMC216526
SummaryPage BrowsePDF–1.0M

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