Distal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase: ARGININE BUT NOT ASPARTATE IS ESSENTIAL FOR PEROXIDASE ACTIVITY - Wikidata - awgldk - TriplyDB

Distal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase: ARGININE BUT NOT ASPARTATE IS ESSENTIAL FOR PEROXIDASE ACTIVITY

Distal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase: ARGININE BUT NOT ASPARTATE IS ESSENTIAL FOR PEROXIDASE ACTIVITY

http://www.wikidata.org/entity/Q27677091

about

First Crystal Structure of a Fungal High-redox Potential Dye-decolorizing Peroxidase: SUBSTRATE INTERACTION SITES AND LONG-RANGE ELECTRON TRANSFER Improved Manganese-Oxidizing Activity of DypB, a Peroxidase from a Lignolytic Bacterium Independent evolution of four heme peroxidase superfamilies Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme Characterization of Dye-decolorizing Peroxidase (DyP) from Thermomonospora curvata Reveals Unique Catalytic Properties of A-type DyPs.Characterization of a Mycobacterium tuberculosis nanocompartment and its potential cargo proteins Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase.Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ).DyP-type peroxidases: a promising and versatile class of enzymes.Chlorite dismutases - a heme enzyme family for use in bioremediation and generation of molecular oxygen.Expression, purification and crystallization of a dye-decolourizing peroxidase from Dictyostelium discoideum.Biotechnological and Biochemical Utilization of Lignin.Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.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.Reducing biomass recalcitrance by heterologous expression of a bacterial peroxidase in tobacco (Nicotiana benthamiana).Active Sites of O2-Evolving Chlorite Dismutases Probed by Halides and Hydroxides and New Iron-Ligand Vibrational Correlations.O2 -independent demethylation of trimethylamine N-oxide by Tdm of Methylocella silvestris.Surface enhanced resonance Raman detection of a catalytic intermediate of DyP-type peroxidase Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage

P2860

Q27675457-547AF558-B721-45D5-9FBD-19A8C5A38711 Q27675863-975987E8-C059-4817-A6DD-3D1A096163DC Q28648029-BC463C5A-81EB-489C-B0A0-55C083572C3D Q30152968-E7C1F48A-E116-4E39-9C64-7B1D4EA7E479 Q30982363-1BCD0D50-C23F-435C-B46B-B7C6E2C9B308 Q34073938-C0150799-9F92-4864-8FB4-57001D94D03E Q35323100-B8816F6E-D754-4A86-8F28-C2DDAA3B5ED6 Q37696971-530DE299-3DA8-4F1F-B8BF-D150FB1316A0 Q38161320-81118C1F-15A1-48B4-A5BA-674B4A684559 Q38187384-DC57168E-4161-4830-B060-8C7B4F37E5DF Q38308358-6135D9A4-A2CE-40AC-BA2F-B04CC10B5516 Q38679535-6971E291-3E45-4082-BDE2-23736923AEFD Q39138975-DB8CB2B8-E319-4F88-8230-4DBBCC443024 Q39392137-3D4C7729-93AE-4469-A644-896797FBCEEC Q39418916-2558EEF6-18ED-4F13-A489-4DA47FCE2538 Q47125715-6C7C1296-2DF4-40F9-984F-7CA8E9664406 Q48010244-78A3E73B-E2FD-4C68-B89A-BF3FD9970F72 Q51490483-E17FCB22-227F-4F9B-812A-08FBAC735725 Q57654060-0B52989C-0F9A-4622-A06B-C323F757ECEA Q58802667-E00E88D5-1901-4A29-B646-B9C92EDF70BD

P2860

Distal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase: ARGININE BUT NOT ASPARTATE IS ESSENTIAL FOR PEROXIDASE ACTIVITY

http://www.wikidata.org/entity/Q27677091

description

2012 nî lūn-bûn

@nan

2012 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի մարտին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@ast

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@en

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@nl

type

label

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@ast

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@en

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@nl

prefLabel

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@ast

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@en

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@nl

P1433

Q27677091-C96B8236-B318-4641-919B-A87679872450

P1476

Q27677091-DCAA70F4-07F4-4368-9B96-D4F7EA5210D8

P2093

Q27677091-BBA8438D-4065-43E1-9837-AF6A5C389D95

Q27677091-CE844750-8280-4A89-84F4-39EBB0CF13AF

Q27677091-D67DBAB7-4769-473E-82F6-34050B7DF804

Q27677091-DDE27F3F-F70C-45C0-B6D7-8340B1CB48EE

Q27677091-FF97A9F7-BFCE-41C3-ABAD-7377A9EA8020

P2860

Q27677091-06CAE7FB-324A-4B56-86FE-B45F421BFCF4

Q27677091-148677DF-C3B0-4812-9B39-7F7B83BCB929

Q27677091-17E14018-ADC0-4829-B7F7-C5C7AD669FA6

Q27677091-18BDA013-A519-46F1-AB85-D166C8FB662C

Q27677091-1D232665-29BE-4F01-B4B0-8A3B52D535B9

Q27677091-2280F5A0-091E-4C55-84B5-375608D31BFE

Q27677091-253AFEDB-8591-4972-97B4-8AD3B3D786A8

Q27677091-34456F0B-04B5-4F3D-A188-AA48DBA8A512

Q27677091-3A5182A3-48F9-42C1-A364-96DAF6891E39

Q27677091-45DD38D0-EBC8-4E59-89BB-4CFD1E4AFCAF

P304

Q27677091-593FC84D-56BF-4780-863F-E90E0B99CD45

P31

Q27677091-645849A9-14B2-4058-9084-9698C407FAC4

P3181

Q27677091-77A90204-8DD9-4336-8821-E6714E917C53

P356

Q27677091-FA572F2F-77C1-4EDA-A9B6-79A9F4649165

P407

Q27677091-6BCCBF7B-3155-45A0-9FC1-1468D63C1024

P433

Q27677091-6AEF2810-0574-47EA-96DD-69E54DE70475

P478

Q27677091-AC4E2DBF-3D52-4D60-8568-5AA9AA86DB59

P577

Q27677091-4CCAABBD-B6CE-4A7C-BFBC-65945ACA763B

P698

Q27677091-59549816-2E83-4C9A-8168-2447A7C90507

P921

Q27677091-36506DEC-9B5B-40FD-8F9E-6F3E22F85DE0

P932

Q27677091-EDDF4C27-4122-4EE5-A1A4-6C881EAC6C32

P3181

P356

JBC.M111.332171

P1433

Journal of Biological Chemistry

P1476

Distal Heme Pocket Residues of ...... ENTIAL FOR PEROXIDASE ACTIVITY

@en

P2093

Jason C Grigg

http://www.w3.org/2001/XMLSchema#string

Lindsay D Eltis

http://www.w3.org/2001/XMLSchema#string

Michael E P Murphy

http://www.w3.org/2001/XMLSchema#string

Rahul Singh

http://www.w3.org/2001/XMLSchema#string

Zachary Armstrong

http://www.w3.org/2001/XMLSchema#string

P2860

Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of the ascorbate peroxidase-ascorbate complex

Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif

Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA

Crystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157

Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1

Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism

Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide

The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid

P304

10623-30

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

3665754

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.M111.332171

http://www.w3.org/2001/XMLSchema#string

P407

P433

13

http://www.w3.org/2001/XMLSchema#string

P478

287

http://www.w3.org/2001/XMLSchema#string

P577

2012-03-23T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

22308037

http://www.w3.org/2001/XMLSchema#string

P921

P932

3323036

http://www.w3.org/2001/XMLSchema#string