The Radical SAM enzyme NirJ catalyzes the removal of two propionate side chains during heme d1 biosynthesis.

about

The Radical SAM enzyme NirJ catalyzes the removal of two propionate side chains during heme d1 biosynthesis.

Item

http://www.wikidata.org/entity/Q50094595

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

The Radical SAM enzyme NirJ ca ...... s during heme d1 biosynthesis.

@en

The Radical SAM enzyme NirJ ca ...... s during heme d1 biosynthesis.

@nl

type

Item

label

The Radical SAM enzyme NirJ ca ...... s during heme d1 biosynthesis.

@en

The Radical SAM enzyme NirJ ca ...... s during heme d1 biosynthesis.

@nl

prefLabel

The Radical SAM enzyme NirJ ca ...... s during heme d1 biosynthesis.

@en

The Radical SAM enzyme NirJ ca ...... s during heme d1 biosynthesis.

@nl

P1476

The Radical SAM enzyme NirJ ca ...... ns during heme d1 biosynthesis

@en

P2093

Gunhild Layer

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

Linda Boss

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

Ramona Oehme

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

Susan Billig

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

P2860

The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri

Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods

Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes

Salmonella typhimurium cobalamin (vitamin B12) biosynthetic genes: functional studies in S. typhimurium and Escherichia coli

SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes

Auxiliary iron-sulfur cofactors in radical SAM enzymes

Crystal Structure of the Heme d 1 Biosynthesis Enzyme NirE in Complex with Its Substrate Reveals New Insights into the Catalytic Mechanism of S -Adenosyl-l-methionine-dependent Uroporphyrinogen III Methyltransferases

X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification

X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry

The crystal structure of siroheme decarboxylase in complex with iron-uroporphyrin III reveals two essential histidine residues

P304

4314-4327

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

P31

scholarly article

P356

10.1111/FEBS.14307

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

P407

English

P433

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

P478

284

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

P50

Claudia Birkemeyer

P577

2017-11-15T00:00:00Z

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

P698

29076625

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