A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate

Biochemistry

Volumn 48, Issue 5, 2009, Pages 951-959

  Ostrander, Elizabeth L ^a   Larson, John D ^a   Schuermann, Jonathan P ^c   Tanner, John J ^a,b  

^a UNIVERSITY OF MISSOURI   (United States)

^b University of Missouri   (United States)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; CATALYTIC EFFICIENCIES; GAIN INSIGHTS; HYDROXYL GROUPS; KINETICS MEASUREMENTS; L PROLINES; POTENTIAL SUBSTRATES; PROLINE DEHYDROGENASE; SERINE RESIDUES; SIDE CHAINS; STRUCTURAL DETERMINANTS; SUBSTRATE BINDINGS; SUBSTRATE SPECIFICITIES; TYROSINE RESIDUES;

AMINO ACIDS; ANIMAL CELL CULTURE; CARBOXYLATION; ENZYMES; ESCHERICHIA COLI; HYDROGEN; HYDROGEN BONDS; PHENOLS;

SUBSTRATES;

2 FUROIC ACID DERIVATIVE; ALANINE; ESCHERICHIA COLI PROTEIN; HYDROXYL GROUP; HYDROXYPROLINE; PROLINE; PROLINE DEHYDROGENASE; PUTA ENZYME; SERINE; TETRAHYDRO 2 FUROIC ACID; TYROSINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; MEMBRANE PROTEIN; PUTA PROTEIN, BACTERIA;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROGEN BOND; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; AMINO ACID SEQUENCE; CHEMISTRY; COMPARATIVE STUDY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; HUMANS; HYDROXYPROLINE; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROLINE; PROLINE OXIDASE; SUBSTRATE SPECIFICITY; TYROSINE;

EID: 61449176891     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802094k     Document Type: Article

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