Analysis of the substrate specificity loop of the HAD superfamily cap domain
about
The Enzyme Function Initiative.The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition stateAnalysis of the Structural Determinants Underlying Discrimination between Substrate and Solvent in β-Phosphoglucomutase Catalysis † ‡The Tail of KdsC: CONFORMATIONAL CHANGES CONTROL THE ACTIVITY OF A HALOACID DEHALOGENASE SUPERFAMILY PHOSPHATASEStructural Determinants of Substrate Recognition in the HAD Superfamily Member d - glycero - d - manno -Heptose-1,7-bisphosphate Phosphatase (GmhB),Discovery of a glycerol 3-phosphate phosphatase reveals glycerophospholipid polar head recycling in Mycobacterium tuberculosisEvolutionary and Structural Analyses of Mammalian Haloacid Dehalogenase-type Phosphatases AUM and Chronophin Provide Insight into the Basis of Their Different Substrate SpecificitiesMarine Rhodobacteraceae L-haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic waterHigh-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutasesAn FMN hydrolase is fused to a riboflavin kinase homolog in plantsSublethal detergent concentrations increase metabolization of recalcitrant polyphosphonates by the cyanobacterium Spirulina platensis.Polynucleotide kinase as a potential target for enhancing cytotoxicity by ionizing radiation and topoisomerase I inhibitorsThe kinetic analysis of the substrate specificity of motif 5 in a HAD hydrolase-type phosphosugar phosphatase of Arabidopsis thaliana.Phosphodiester cleavage in ribonuclease H occurs via an associative two-metal-aided catalytic mechanism.Farnesyl phosphatase, a Corpora allata enzyme involved in juvenile hormone biosynthesis in Aedes aegypti.Alternative pathways for phosphonate metabolism in thermophilic cyanobacteria from microbial mats.Deletion of PHO13, encoding haloacid dehalogenase type IIA phosphatase, results in upregulation of the pentose phosphate pathway in Saccharomyces cerevisiae.A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site.Panoramic view of a superfamily of phosphatases through substrate profilingPromiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Isolation and characterization of Xenorhabdus nematophila transposon insertion mutants defective in lipase activity against TweenCharacterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis.Catalytic scaffolds for phosphoryl group transfer.HAD hydrolase function unveiled by substrate screening: enzymatic characterization of Arabidopsis thaliana subclass I phosphosugar phosphatase AtSgpp.Diversification of function in the haloacid dehalogenase enzyme superfamily: The role of the cap domain in hydrolytic phosphoruscarbon bond cleavage.Yihx-encoded haloacid dehalogenase-like phosphatase HAD4 from Escherichia coli is a specific α-d-glucose 1-phosphate hydrolase useful for substrate-selective sugar phosphate transformations.YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate x) hydrolase superfamily.The α-Phosphoglucomutase ofLactococcus lactisIs Unrelated to the α-d-Phosphohexomutase Superfamily and Is Encoded by the Essential GenepgmH
P2860
Q24628703-EB735A3E-C00B-43D9-B46A-C212466F904FQ27650273-1CEAFB4A-8B29-436B-9FCB-4CC1C1AFD075Q27653467-54EF9D29-82C1-47EE-A057-4FAED9788767Q27657281-D75E8448-D51C-420F-BDF7-B05F59595C5FQ27658852-35F8806C-8DA3-465D-8DA2-93B2E03C55B4Q27678803-851A81CE-9128-4355-88A7-43E6CD74B1DFQ27680884-31897D28-3285-44A8-A5C6-DB77CE8DA3C5Q27683918-14680EE0-B33C-4924-ABC2-9366AF8FCD71Q27686984-37C52552-CD36-4F04-A81E-0723396CBD0CQ28273904-8F5E6CD0-55A7-4982-BCA7-DA6EB9927DCEQ30574439-C8F6EC03-5301-4814-83D7-44632F0E4C89Q34231660-48308437-A722-4DDF-B036-4E59B9735C94Q34423972-47E2423E-60CC-4E70-BD56-53D26D623205Q34801870-C180FF51-F475-4B5E-9B44-489678ACCF20Q34938188-00524543-57CB-4728-8842-18BBEB31764AQ35018582-27F67B87-43C6-4748-AE99-6CB50D57A18CQ35075084-852DA257-7CEB-4DA5-8070-4325C2BE111CQ35075447-0C753BD7-9CBF-4479-8506-BE48AAB72770Q35549038-46017BED-7657-4F05-AD1F-D1CAF262F55AQ36019839-62897232-C056-4E9D-A3D4-274D868F5243Q37301967-7A9EEC9B-DE30-4922-A5A2-B971226F2328Q38922759-22F565CB-5883-4FAF-8034-F09B6EC6FE5AQ38928103-80E8F6CE-A642-4B02-93F0-4B54A6ED7C41Q39282811-CCB2E692-F8D0-4DAE-811E-AF7F6A2535E9Q42425228-F695F1D1-F07A-4B8D-9040-9C6C3A5C5C6CQ43050391-B7CF771A-C4A8-4D15-A88D-8AEB2B0E77C1Q43178629-FA3B4C6B-3526-4E89-8AA9-1F212B99F674Q57881750-D33807E8-700B-462F-AB5C-3AC8F57FC23F
P2860
Analysis of the substrate specificity loop of the HAD superfamily cap domain
description
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2004
@ast
im März 2004 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/03/16)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/03/16)
@nl
наукова стаття, опублікована в березні 2004
@uk
مقالة علمية (نشرت في 16-3-2004)
@ar
name
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@ast
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@en
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@nl
type
label
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@ast
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@en
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@nl
prefLabel
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@ast
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@en
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@nl
P2093
P3181
P356
P1433
P1476
Analysis of the substrate specificity loop of the HAD superfamily cap domain
@en
P2093
Guofeng Zhang
Jianying Dai
Karen N. Allen
Sushmita D. Lahiri
P304
P3181
P356
10.1021/BI0356810
P407
P577
2004-03-16T00:00:00Z