Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
about
CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activityStructure-Guided Discovery of Phenyl-diketo Acids as Potent Inhibitors of M. tuberculosis Malate SynthaseThe crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthasesMycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product ExchangeHijacking and Use of Host Lipids by Intracellular Pathogens.Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation in Mycobacterium tuberculosis.
P2860
Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
description
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2011 թվականի օգոստոսին հրատարակված գիտական հոդված
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artículu científicu espublizáu en 2011
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im August 2011 veröffentlicher wissenschaftlicher Artikel
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scientific journal article
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wetenschappelijk artikel (gepubliceerd op 2011/08/16)
@nl
наукова стаття, опублікована в серпні 2011
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مقالة علمية (نشرت في 16-8-2011)
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name
Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
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Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
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type
label
Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
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Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
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prefLabel
Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
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Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
@en
P2860
P356
P1433
P1476
Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis
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P2093
Christine E. Quartararo
John S. Blanchard
P2860
P304
P356
10.1021/BI2007299
P407
P577
2011-08-16T00:00:00Z