Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
about
A critical role for the histidine residues in the catalytic function of acyl-CoA:cholesterol acyltransferase catalysis: evidence for catalytic difference between ACAT1 and ACAT2Molecular bases of catalysis and ADP-ribose preference of human Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase and conversion by mutagenesis to a preferential cyclic ADP-ribose phosphohydrolaseMalonate-bound structure of the glycerophosphodiesterase fromEnterobacter aerogenes(GpdQ) and characterization of the native Fe2+metal-ion preferenceSubstrate-Promoted Formation of a Catalytically Competent Binuclear Center and Regulation of Reactivity in a Glycerophosphodiesterase from Enterobacter aerogenesCrystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosaCharacterization of Danio rerio Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family.A molecular description of acid phosphatase.The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysisIdentification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferases 1A.Selective Coordination of Gallium(III), Zinc(II), and Copper(II) by an Asymmetric Dinucleating Ligand: A Model for Metallophosphatases.Monoesterase Activity of a Purple Acid Phosphatase Mimic with a Cyclam Platform
P2860
Q24322278-B21EC8DD-0612-48DD-BB49-8610D0DDF613Q27313411-76FF3EAC-06F1-4363-B9A2-65C24D6B454BQ27651414-5667F60C-0102-4F62-8A0B-B71C98DABE2CQ27652378-702C5219-8A77-4C59-81A8-7629E81DDCA5Q30090132-25093096-E9F3-4D94-93C3-0D64A2CE5544Q34359672-2FF1354E-E0F7-4EBC-8C5B-4A9E46363902Q38017593-BBD632E0-FEFD-40B2-A03A-EA588FF66D89Q41459135-718705CC-4214-4669-AC90-4BC6713B8D8FQ46935096-C2A8AE6F-ECD2-491D-8C3A-95AF1021C724Q53424815-3B477CB5-6C4B-49BA-8FAB-BF52EBA42B96Q59326560-D11F5943-D311-438F-A186-8C2936E6D9F8
P2860
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
description
2005 nî lūn-bûn
@nan
2005年の論文
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2005年学术文章
@wuu
2005年学术文章
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2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
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2005年學術文章
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name
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
@en
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
@nl
type
label
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
@en
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
@nl
prefLabel
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
@en
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
@nl
P2093
P2860
P1433
P1476
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
@en
P2093
Bruce A Averill
Enrico G Funhoff
Goran Andersson
Yunling Wang
P2860
P304
P356
10.1111/J.1742-4658.2005.04686.X
P407
P577
2005-06-01T00:00:00Z