Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase. Examination of the role of this residue in coenzyme-binding and catalysis.

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Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase. Examination of the role of this residue in coenzyme-binding and catalysis.

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http://www.wikidata.org/entity/Q48568725

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1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年学术文章

@wuu

1996年学术文章

@zh

1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

1996年學術文章

@zh-hant

name

Carboxymethylation of MutS-cys ...... oenzyme-binding and catalysis.

@en

Carboxymethylation of MutS-cys ...... oenzyme-binding and catalysis.

@nl

type

Item

label

Carboxymethylation of MutS-cys ...... oenzyme-binding and catalysis.

@en

Carboxymethylation of MutS-cys ...... oenzyme-binding and catalysis.

@nl

prefLabel

Carboxymethylation of MutS-cys ...... oenzyme-binding and catalysis.

@en

Carboxymethylation of MutS-cys ...... oenzyme-binding and catalysis.

@nl

P1476

Carboxymethylation of MutS-cys ...... oenzyme-binding and catalysis.

@en

P2093

E N Marsh

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

H P Chen

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P2860

How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase

The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme

How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution

A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes

Cloning, sequencing and expression of the gene encoding the coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri in Escherichia coli.

The mechanism of adenosylcobalamin-dependent reactions.

Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity.

Protein radical involvement in biological catalysis?

Cobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymes.

A radical approach to enzyme catalysis.

P304

29121-29125

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P31

scholarly article

P356

10.1074/JBC.271.46.29121

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P407

English

P433

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

P478

271

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P50

Daniel E. Holloway

P577

1996-11-01T00:00:00Z

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P5875

14295654

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P698

8910568

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