Collagen prolyl 4-hydroxylase tetramers and dimers show identical decreases in Km values for peptide substrates with increasing chain length: Mutation of one of the two catalytic sites in the tetramer inactivates the enzyme by more than half

Journal of Biological Chemistry

Volumn 279, Issue 18, 2004, Pages 18656-18661

  Kukkola, Liisa ^a   Koivunen, Peppi ^a   Pakkanen, Outi ^a   Page, Antony P ^b   Myllyharju, Johanna ^a  

^a UNIVERSITY OF OULU   (Finland)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DIMERS; ENZYMES; SUBSTRATES;

PEPTIDE SUBSTRATES; TETRAMERS;

BIOCHEMISTRY;

2 OXOGLUTARIC ACID; COLLAGEN; DIMER; FERROUS ION; PEPTIDE; POLYPEPTIDE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN DISULFIDE ISOMERASE; TETRAMER;

ANIMAL CELL; ARTICLE; BETA CHAIN; BINDING SITE; CAENORHABDITIS ELEGANS; CATALYSIS; ENZYME INACTIVATION; ENZYME SUBSTRATE COMPLEX; EXTRACELLULAR MATRIX; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING;

AMINO ACID SUBSTITUTION; ANIMALS; CAENORHABDITIS ELEGANS PROTEINS; CATALYTIC DOMAIN; DIMERIZATION; HUMANS; HYDROXYLATION; KINETICS; PEPTIDES; PROCOLLAGEN-PROLINE DIOXYGENASE; PROTEIN ISOFORMS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; SUBSTRATE SPECIFICITY;

ANIMALIA; CAENORHABDITIS; CAENORHABDITIS ELEGANS; VERTEBRATA;

EID: 2442572125     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401514200     Document Type: Article

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