Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation

ChemBioChem

Volumn 9, Issue 9, 2008, Pages 1439-1449

  Lisurek, Michael ^a   Simgen, Birgit ^a   Antes, Iris ^b   Bernhardt, Rita ^a  

^a SAARLAND UNIVERSITY   (Germany)

^b MAX PLANCK INSTITUTE FOR INFORMATICS   (Germany)

Author keywords

Cytochromes; Hydroxylases; Molecular modeling; Mutagenesis; Steroids

Indexed keywords

ALDOSTERONE SYNTHASE; CYTOCHROME P450; CYTOCHROME P450 101; CYTOCHROME P450 106A2; CYTOCHROME P450 107A1; CYTOCHROME P450 108; CYTOCHROME P450 119; CYTOCHROME P450 55A1; DEOXYCORTICOSTERONE; MUTANT PROTEIN; PROGESTERONE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; HEME; RECOMBINANT PROTEIN; STEROID MONOOXYGENASE;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; MOLECULAR DOCKING; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ALIGNMENT; STEREOCHEMISTRY; STEROID HYDROXYLATION; WILD TYPE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION REGULATION; GENETICS; HUMAN; HYDROXYLATION; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STEREOISOMERISM;

BACTERIA (MICROORGANISMS);

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYSIS; ENZYME STABILITY; GENE EXPRESSION REGULATION, BACTERIAL; HEME; HUMANS; HYDROXYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; OXIDATION-REDUCTION; PROGESTERONE; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STEREOISOMERISM; STEROID HYDROXYLASES; SUBSTRATE SPECIFICITY;

EID: 49249113945     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200700670     Document Type: Article

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