Identification of a human trans-3-hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes

Journal of Biological Chemistry

Volumn 287, Issue 26, 2012, Pages 21654-21662

  Visser, Wouter F ^a   Verhoeven Duif, Nanda M ^a   De Koning, Tom J ^a  

^a UNIVERSITY MEDICAL CENTER UTRECHT   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BASEMENT MEMBRANE; CYSTEINE RESIDUES; ENZYMATIC ACTIVITIES; FREE PROLINE; HUMAN ENZYMES; HUMAN PROTEINS; MUTANT ENZYMES; RACEMASE ACTIVITY; SINGLE RESIDUE; STRUCTURAL COMPONENT; THREONINE RESIDUES;

CARBOXYLATION; DEGRADATION; ENZYMES; GENES; PROTEINS;

AMINO ACIDS;

3 HYDROXY PROLINE DEHYDRATASE; 3 HYDROXYPROLINE EPIMERASE; CARBOXYLIC ACID DERIVATIVE; CYSTEINE; EPIMERASE; ISOMERASE; PROTEIN C14ORF149; PYRROLINE 2 CARBOXYLIC ACID; RACEMASE; THREONINE; UNCLASSIFIED DRUG;

AMINO ACID METABOLISM; ARTICLE; BIOCATALYSIS; C14ORF149 GENE; CONTROLLED STUDY; DEHYDRATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE COMPLEX; GENE; HUMAN; HUMAN TISSUE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION;

AMINO ACID ISOMERASES; ANIMALS; BASEMENT MEMBRANE; CARBON-OXYGEN LYASES; CATALYSIS; CATALYTIC DOMAIN; CLONING, MOLECULAR; CYSTEINE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE TRANSFERASE; HUMANS; HYDROXYPROLINE; MODELS, BIOLOGICAL; MUTATION; OPEN READING FRAMES; PHYLOGENY; POLYMERASE CHAIN REACTION; TISSUE DISTRIBUTION;

EID: 84862638274     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.363218     Document Type: Article

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