DyP-type peroxidases comprise a novel heme peroxidase family.
about
A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamilyMolecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residueFirst Crystal Structure of a Fungal High-redox Potential Dye-decolorizing Peroxidase: SUBSTRATE INTERACTION SITES AND LONG-RANGE ELECTRON TRANSFERImproved Manganese-Oxidizing Activity of DypB, a Peroxidase from a Lignolytic BacteriumDistal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase: ARGININE BUT NOT ASPARTATE IS ESSENTIAL FOR PEROXIDASE ACTIVITYManipulating Conserved Heme Cavity Residues of Chlorite Dismutase: Effect on Structure, Redox Chemistry, and ReactivityAnabaena sp. DyP-type peroxidase is a tetramer consisting of two asymmetric dimersAnti-schistosomal intervention targets identified by lifecycle transcriptomic analysesTime-scale dynamics of proteome and transcriptome of the white-rot fungus Phlebia radiata: growth on spruce wood and decay effect on lignocelluloseIndependent evolution of four heme peroxidase superfamiliesIron homeostasis in the Rhodobacter genusDescription of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)Characterization of Dye-decolorizing Peroxidase (DyP) from Thermomonospora curvata Reveals Unique Catalytic Properties of A-type DyPs.Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli.Metagenomic analysis of a tropical composting operation at the são paulo zoo park reveals diversity of biomass degradation functions and organismsApplication of a novel alkali-tolerant thermostable DyP-type peroxidase from Saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp.The Escherichia coli protein YfeX functions as a porphyrinogen oxidase, not a heme dechelataseRoles of reactive oxygen species-degrading enzymes of Francisella tularensis SCHU S4Characterization of SfmD as a Heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis.Identification of a Novel Dye-Decolorizing Peroxidase, EfeB, Translocated by a Twin-Arginine Translocation System in Streptococcus thermophilus CGMCC 7.179.Evolutionary relationships between heme-binding ferredoxin α + β barrels.Extracellular proteins of Trametes hirsuta st. 072 induced by copper ions and a lignocellulose substrate.Characterization of a novel dye-decolorizing peroxidase (DyP)-type enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw.Bacteria capture iron from heme by keeping tetrapyrrol skeleton intactActinobacterial peroxidases: an unexplored resource for biocatalysis.Adventures in Rhodococcus - from steroids to explosives.The iron-regulated staphylococcal lipoproteins.DyP-type peroxidases: a promising and versatile class of enzymes.The ligninolytic peroxidases in the genus Pleurotus: divergence in activities, expression, and potential applications.Expression, purification and crystallization of a dye-decolourizing peroxidase from Dictyostelium discoideum.Biotechnological and Biochemical Utilization of Lignin.New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications.Chemistry and Molecular Dynamics Simulations of Heme b-HemQ and Coproheme-HemQ.Anthraquinone dyes decolorization capacity of anamorphic Bjerkandera adusta CCBAS 930 strain and its HRP-like negative mutants.Actinobacteria isolated from termite guts as a source of novel oxidative enzymes.Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus.Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study.Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamilyIdentification and molecular characterization of a novel DyP-type peroxidase from Pseudomonas aeruginosa PKE117.
P2860
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P2860
DyP-type peroxidases comprise a novel heme peroxidase family.
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
DyP-type peroxidases comprise a novel heme peroxidase family.
@ast
DyP-type peroxidases comprise a novel heme peroxidase family.
@en
DyP-type peroxidases comprise a novel heme peroxidase family.
@nl
type
label
DyP-type peroxidases comprise a novel heme peroxidase family.
@ast
DyP-type peroxidases comprise a novel heme peroxidase family.
@en
DyP-type peroxidases comprise a novel heme peroxidase family.
@nl
prefLabel
DyP-type peroxidases comprise a novel heme peroxidase family.
@ast
DyP-type peroxidases comprise a novel heme peroxidase family.
@en
DyP-type peroxidases comprise a novel heme peroxidase family.
@nl
P1476
DyP-type peroxidases comprise a novel heme peroxidase family.
@en
P2093
P2888
P304
P356
10.1007/S00018-008-8651-8
P577
2009-04-01T00:00:00Z