Role of the main access channel of catalase-peroxidase in catalysis. - Wikidata - wikimedia - TriplyDB

Role of the main access channel of catalase-peroxidase in catalysis.

Role of the main access channel of catalase-peroxidase in catalysis.

http://www.wikidata.org/entity/Q50122764

about

An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalase-peroxidase (KatG)Molecular dynamics simulations: advances and applications Radical sites in Mycobacterium tuberculosis KatG identified using electron paramagnetic resonance spectroscopy, the three-dimensional crystal structure, and electron transfer couplings MolAxis: a server for identification of channels in macromolecules Role of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant.Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.The One-electron Autoxidation of Human Cytochrome P450 3A4 Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism

P2860

Q24644161-84F909CF-ED66-43C9-BC9A-7BAA5732BC32 Q26775869-55B1227A-67ED-4EA3-A52D-E754F268138C Q35829950-BE0178F7-DD30-4502-84AD-A7E48E64EC70 Q36749375-475F392A-EE40-42D5-98CD-3DF12177B188 Q43167115-93945830-D643-4428-B543-005D8A87B0DA Q46296304-81125CCF-15A6-4CFD-812D-6AFBE1515241 Q52677195-3431DAF4-B2EE-4BE4-8C84-0CED2C9BB445 Q58035712-12A1A221-B18B-4372-A430-FC8C40ED1511 Q59053158-CA21383D-B17C-434D-ADB2-7CE27F3BD972

P2860

Role of the main access channel of catalase-peroxidase in catalysis.

http://www.wikidata.org/entity/Q50122764

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

Role of the main access channel of catalase-peroxidase in catalysis.

@en

Role of the main access channel of catalase-peroxidase in catalysis.

@nl

type

label

Role of the main access channel of catalase-peroxidase in catalysis.

@en

Role of the main access channel of catalase-peroxidase in catalysis.

@nl

prefLabel

Role of the main access channel of catalase-peroxidase in catalysis.

@en

Role of the main access channel of catalase-peroxidase in catalysis.

@nl

P1433

Q50122764-1E02EF77-29A4-47A9-9C94-460141D80A77

P1476

Q50122764-238FBE6E-1C38-4B93-8167-89982EFB8B1A

P2093

Q50122764-57520813-0ADC-4663-8983-50DDD67CBF6B

Q50122764-AC2A0B34-48F1-43F3-8B06-24E491AF47D9

P2860

Q50122764-0601CA23-56ED-49D8-A134-BCEF66F7C839

Q50122764-09BC96C4-0ECF-4EB2-8D6E-0BFF14885389

Q50122764-0C0389F0-28DF-4DF4-8428-AC28FB9789A5

Q50122764-14EE37C3-09B1-4D58-8F53-E7C0023017EA

Q50122764-24A339B6-E850-49AD-B7F5-000A3FFF90F8

Q50122764-27A6ABF0-C866-4396-84FE-887F625DC2D9

Q50122764-29585F46-4CA5-446E-B646-B6A0A925B700

Q50122764-49FF1848-B4BE-4148-B4E2-D1AF3FB8404A

Q50122764-4D29CC8A-DCA2-401F-B75D-4EC5D1DCBA4B

Q50122764-50FF19C2-9A9D-4CB5-A01E-179B48B511AD

P304

Q50122764-7F593306-80B3-457D-921D-D0DDB97492A3

P31

Q50122764-7D33B81D-5835-403E-9425-DCFAB9AE3FC6

P356

Q50122764-39EFAA39-2BF9-4A4C-A74E-09CA1254C19D

P407

Q50122764-0A54D2FF-548F-4F8C-A281-2BEC54D6657D

P433

Q50122764-6AB33F1F-0C8A-4367-9FAF-800147EA9A01

P478

Q50122764-28AB8C37-3337-424B-80DE-DE44B0F384A4

P50

Q50122764-47DD1B7F-2E2C-4396-960F-24BCB96E8782

Q50122764-6E3E447D-788B-43EB-8814-B0023CCDCBF0

Q50122764-A7BEAB9B-AE35-4900-B41E-E68877BF5B76

Q50122764-CDFD34FF-B838-4081-8BBF-5586024E5DBE

P577

Q50122764-08AA69A0-A79E-4096-90F7-785E9EDBFD8B

P5875

Q50122764-9F49DB22-91D7-440B-ADD7-F9F4F6C7F41E

P698

Q50122764-BCCF23A3-21A5-4414-A979-577B0141BFBE

P356

P1433

Journal of Biological Chemistry

P1476

Role of the main access channel of catalase-peroxidase in catalysis.

@en

P2093

Enrica Droghetti

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

Florian Schmuckenschlager

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

P2860

Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism

Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli

The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui

Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution

An electrical potential in the access channel of catalases enhances catalysis

Structure of catalase-A from Saccharomyces cerevisiae

Calculation of protein extinction coefficients from amino acid sequence data

Crystal structure of Mycobacterium tuberculosis catalase-peroxidase

Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned?

Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization.

P304

42411-42422

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

P31

scholarly article

P356

10.1074/JBC.M508009200

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

P407

P433

51

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

P478

280

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

P50

Giulietta Smulevich

Paul G. Furtmüller

Christian Obinger

Christa Jakopitsch

P577

2005-10-22T00:00:00Z

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

P5875

7522946

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

P698

16244360

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