DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases

Journal of Biological Chemistry

Volumn 282, Issue 50, 2007, Pages 36652-36658

  Sugano, Yasushi ^a   Muramatsu, Riichi ^a   Ichiyanagi, Atsushi ^a   Sato, Takao ^a   Shoda, Makoto ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE RESIDUE; HOMOLOGY; PLANT PEROXIDASES;

CRYSTAL STRUCTURE; FUNGI; SPECTROPHOTOMETRY;

ENZYME ACTIVITY;

ARGININE; ASPARTIC ACID; CATION; DYE; HEME; HISTIDINE; MONOPHENOL MONOOXYGENASE; PEROXIDASE; PORPHYRIN; PROTEIN CPOP21; PROTEIN DYP; PROTEIN TAP; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; DECOLORIZATION; ENZYME STRUCTURE; FUNGUS; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN TERTIARY STRUCTURE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; THANATEPHORUS CUCUMERIS;

BASIDIOMYCOTA; BINDING SITES; FUNGAL PROTEINS; HEME; HEMEPROTEINS; IRON; MONOPHENOL MONOOXYGENASE; PEROXIDASE; PHYLOGENY; PROTEIN STRUCTURE, QUATERNARY; STRUCTURAL HOMOLOGY, PROTEIN;

FUNGI; THANATEPHORUS CUCUMERIS;

EID: 37549031745     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M706996200     Document Type: Article

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