Structural basis for the catalytic mechanism of aspartate ammonia lyase

Biochemistry

Volumn 50, Issue 27, 2011, Pages 6053-6062

  Fibriansah, Guntur ^a   Veetil, Vinod Puthan ^b   Poelarends, Gerrit J ^b   Thunnissen, Andy Mark W H ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMMONIA LYASE; ASPARTASE; ASPARTATES; BACILLUS SP; C-TERMINAL DOMAINS; CARBOXYLATE GROUPS; CATALYTIC BASE; CATALYTIC MECHANISMS; CONFORMATIONAL CHANGE; FUMARATES; HIGH ENERGY; KINETIC ANALYSIS; LOOP RESIDUES; OPEN CONFORMATION; REACTION MECHANISM; SITE DIRECTED MUTAGENESIS; STRUCTURAL BASIS; SUBSTRATE BINDING;

AMMONIA; BACTERIOLOGY; CARBOXYLATION; CATALYSIS; CATALYST ACTIVITY; ENZYME ACTIVITY; HYDROGEN BONDS; MUTAGENESIS; PLANTS (BOTANY); QUANTUM CHEMISTRY;

SUBSTRATES;

ASPARTATE AMMONIA LYASE;

ARTICLE; BACILLUS; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMMONIA; ASPARTATE AMMONIA-LYASE; BACILLUS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; FUMARATES; LIGANDS; MULTIGENE FAMILY; PROTEIN BINDING; PROTEIN CONFORMATION; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; SERINE; SUBSTRATE SPECIFICITY;

BACILLUS SP.;

EID: 79959988394     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200497y     Document Type: Article

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