The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans

The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans

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http://www.wikidata.org/entity/Q27622443
Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulenceStructure and Function of PA4872 from Pseudomonas aeruginosa , a Novel Class of Oxaloacetate Decarboxylase from the PEP Mutase/Isocitrate Lyase SuperfamilyStructure of Oxalacetate Acetylhydrolase, a Virulence Factor of the Chestnut Blight FungusPotential inhibitors for isocitrate lyase of Mycobacterium tuberculosis and non-M. tuberculosis: a summaryDual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosisResidues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysisIdentification of mannich base as a novel inhibitor of Mycobacterium tuberculosis isocitrate by high-throughput screeningPeroxisome function regulates growth on glucose in the basidiomycete fungus Cryptococcus neoformans.Identification of positive selection in disease response genes within members of the Poaceae.Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamilyGeneration and phenotypic characterization of Aspergillus nidulans methylisocitrate lyase deletion mutants: methylisocitrate inhibits growth and conidiation.2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes.PTS1-independent targeting of isocitrate lyase to peroxisomes requires the PTS1 receptor Pex5p.Gene acquisition, duplication and metabolic specification: the evolution of fungal methylisocitrate lyases.Oxaloacetate hydrolase, the C-C bond lyase of oxalate secreting fungi.Residues Asn214, Gln211, Glu219 and Gln221 contained in the subfamily 3 catalytic signature of the isocitrate lyase from Pseudomonas aeruginosa are involved in its catalytic and thermal properties
P2860

The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans

Item
http://www.wikidata.org/entity/Q27622443
description
2000 nî lūn-bûn
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2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
The crystal structure and acti ...... he fungus Aspergillus nidulans
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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type
label
The crystal structure and acti ...... he fungus Aspergillus nidulans
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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P1476
P2093
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The crystal structure and acti ...... he fungus Aspergillus nidulans
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P2093
P304
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P356
10.1016/S0969-2126(00)00117-9
P433
P478
P50
P577
P698
P921