Reversible post-translational carboxylation modulates the enzymatic activity of N-Acetyl-l-ornithine transcarbamylase

Biochemistry

Volumn 49, Issue 32, 2010, Pages 6887-6895

  Li, Yongdong ^a,b   Yu, Xiaolin ^a   Ho, Jeremy ^a   Fushman, David ^c   Allewell, Norma M ^c   Tuchman, Mendel ^a   Shi, Dashuang ^a  

^a GEORGE WASHINGTON UNIVERSITY   (United States)

^b GANNAN NORMAL UNIVERSITY   (China)

^c Bldg 142   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; ACTIVITY ASSAYS; ARGININE BIOSYNTHESIS; CARBOXYL GROUPS; ELECTRON DENSITIES; ENZYMATIC ACTIVITIES; HUMAN PATHOGENS; HYDROGEN BONDING NETWORK; NMR SPECTROSCOPY; POST-TRANSLATIONAL MODIFICATIONS; SIDE CHAINS; WATER MOLECULE; WILD TYPES; WILD-TYPE ENZYMES; XANTHOMONAS CAMPESTRIS;

AMINO ACIDS; BIOCHEMISTRY; ENZYMES; HYDROGEN BONDS; MOLECULES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

CARBOXYLATION;

CARBOXYL GROUP; GLUTAMIC ACID; HISTIDINE; LYSINE; N ACETYL LEVO ORNITHINE TRANSCARBAMYLASE; N DELTA (PHOSPHONOACETYL) N ALPHA ACETYL LEVO ORNITHINE; ORNITHINE CARBAMOYLTRANSFERASE; ORNITHINE DERIVATIVE; SERINE; UNCLASSIFIED DRUG; WATER;

ARTICLE; BINDING SITE; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXYLATION; CATALYSIS; ENZYME ACTIVITY; HYDROGEN BOND; MUTANT; PRIORITY JOURNAL; PROTEIN PROCESSING; WILD TYPE;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; LYSINE; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; ORNITHINE; ORNITHINE CARBAMOYLTRANSFERASE; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; XANTHOMONAS CAMPESTRIS;

XANTHOMONAS CAMPESTRIS;

EID: 77955571741     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1007386     Document Type: Article

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