Conformational changes in orotidine 5′-monophosphate decarboxylase: "remote" residues that stabilize the active conformation

Biochemistry

Volumn 49, Issue 17, 2010, Pages 3514-3516

  Wood, B McKay ^a   Amyes, Tina L ^b   Fedorov, Alexander A ^c   Fedorov, Elena V ^c   Shabila, Andrew ^a   Almo, Steven C ^c   Richard, John P ^b   Gerlt, John A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CONFORMATIONAL CHANGE; DECARBOXYLASES; HYDROGEN BONDED NETWORK; HYDROPHOBIC RESIDUES; INTRINSIC BINDING; MINIMAL EFFECTS; MONOPHOSPHATES; MUTANT ENZYMES; PHOSPHATE GROUP; RATE ENHANCEMENT; REACTION CATALYZED; STRUCTURAL FACTOR; WILD TYPES;

BINDING ENERGY;

AMINO ACID; HYDROGEN; OROTIDINE 5' PHOSPHATE DECARBOXYLASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; HYDROGEN BOND; HYDROPHOBICITY; METHANOBACTER THERMOAUTOTROPHICUS; METHANOBACTERIUM; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; CATALYSIS; HYDROGEN BONDING; METHANOBACTERIACEAE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; OROTIDINE-5'-PHOSPHATE DECARBOXYLASE; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

METHANOTHERMOBACTER;

EID: 77951677267     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100443a     Document Type: Article

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