Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1

Biochemistry

Volumn 47, Issue 46, 2008, Pages 11964-11972

  Hayashi, Keiko ^a   Sugimoto, Hiroshi ^b   Shinkyo, Raku ^c   Yamada, Masato ^a   Ikeda, Shinnosuke ^a   Ikushiro, Shinichi ^a   Kamakura, Masaki ^a   Shiro, Yoshitsugu ^b   Sakaki, Toshiyuki ^a  

^a TOYAMA PREFECTURAL UNIVERSITY   (Japan)

^b RIKEN SPring 8 Center   (Japan)

^c KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; BINDING ENERGY; BINDING SITES; CHEMICAL REACTIONS; ENZYMES; MOLECULAR INTERACTIONS; ORGANIC ACIDS;

AMINO ACID RESIDUES; DOUBLE MUTANTS; HYDROXYLASE; HYDROXYLATION REACTIONS; KINETIC ANALYSES; REACTION SITES; STRUCTURAL STUDIES; SUBSTRATE SPECIFICITIES; WILD TYPES;

HYDROXYLATION;

CYTOCHROME P450 105A1; MUTANT PROTEIN; OXYGENASE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; STREPTOMYCES; STREPTOMYCES GRISEOLUS; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CALCIFEDIOL; CATALYSIS; CATALYTIC DOMAIN; CYTOCHROME P-450 ENZYME SYSTEM; KINETICS; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY; STREPTOMYCES; SUBSTRATE SPECIFICITY;

STREPTOMYCES GRISEOLUS;

EID: 56249135918     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801222d     Document Type: Article

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