Conserved and non-conserved residues and their role in the structure and function of p-hydroxybenzoate hydroxylase

Protein Engineering, Design and Selection

Volumn 26, Issue 7, 2013, Pages 479-488

  Suemori, Akio ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

FAD; mutant database; NADPH; p hydroxybenzoate hydroxylase; substrate binding

Indexed keywords

CRYSTALLOGRAPHIC STUDIES; FAD; NADPH; P-HYDROXYBENZOATE HYDROXYLASE; PSEUDOMONAS FLUORESCENS; STRUCTURAL CONFORMATIONS; STRUCTURAL STABILITIES; SUBSTRATE BINDING;

AMINO ACIDS; CATALYSIS; ENZYMES; STABILITY;

DATABASE SYSTEMS;

4 HYDROXYBENZOATE 3 MONOOXYGENASE; AMINO ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; COMPUTER PROGRAM; DATA BASE; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS FLUORESCENS;

FAD; MUTANT DATABASE; NADPH; P-HYDROXYBENZOATE HYDROXYLASE; SUBSTRATE BINDING;

4-HYDROXYBENZOATE-3-MONOOXYGENASE; AMINO ACID SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS FLUORESCENS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84880244734     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzt026     Document Type: Article

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