Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis

Journal of Biological Chemistry

Volumn 287, Issue 24, 2012, Pages 20369-20381

  Bisht, Shveta ^a   Rajaram, Venkatesan ^a   Bharath, Sakshibeedu R ^a   Kalyani, Josyula Nitya ^a   Khan, Farida ^a   Rao, Appaji N ^a   Savithri, Handanahal S ^a   Murthy, Mathur R N ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; BIOCHEMISTRY; CATALYSIS; ENZYMES; ESCHERICHIA COLI; PYRIDINE; REACTION INTERMEDIATES; SULFUR COMPOUNDS; SURFACE CHEMISTRY;

BIOLOGICAL INTERFACE; CRYSTALLIZATION CONDITIONS; ENZYME ACTIVATION; MONOCLINIC FORMS; MONOCLINIC STRUCTURES; PLP-DEPENDENT ENZYMES; PYRIDINE RINGS; SITE DIRECTED MUTAGENESIS;

CRYSTAL STRUCTURE;

ASPARTIC ACID; BACTERIAL ENZYME; DIAMINOPROPIONATE AMONNIA LYASE; DISULFIDE; HOMODIMER; LIGAND; LYSINE; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; DENSITY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME MODIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; REGULATORY MECHANISM; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI; PROKARYOTA;

EID: 84862022059     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.351809     Document Type: Article

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