Glutathione biosynthesis in bacteria by bifunctional GshF is driven by a modular structure featuring a novel hybrid ATP-grasp fold

Journal of Molecular Biology

Volumn 416, Issue 4, 2012, Pages 486-494

  Stout, Jan ^a   Vos, Dirk De ^a   Vergauwen, Bjorn ^a   Savvides, Savvas N ^a  

^a GHENT UNIVERSITY   (Belgium)

Author keywords

ATP grasp; bifunctional enzymes; cyanophycin synthetase; glutathione biosynthesis; GshF

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYSTEINE; ENZYME; GAMMA GLUTAMYLCYSTEINE; GLUTAMIC ACID; GLUTATHIONE; GLYCINE; GSHF ENZYME; UNCLASSIFIED DRUG;

ARTICLE; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; CRYSTAL STRUCTURE; ENZYME STRUCTURE; GLUTATHIONE METABOLISM; MUTAGENESIS; NONHUMAN; PASTEURELLA MULTOCIDA; POLYMERIZATION; PRIORITY JOURNAL; STREPTOCOCCUS AGALACTIAE; STRUCTURE ACTIVITY RELATION;

BACTERIA (MICROORGANISMS); PASTEURELLA MULTOCIDA; STREPTOCOCCUS AGALACTIAE;

EID: 84857361072     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.12.046     Document Type: Article

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