(Q51238514)

1 April 2018

title

Survey of catalytic residues and essential roles of glutamate-alpha170 and aspartate-alpha335 in coenzyme B12-dependent diol dehydratase. (English)

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author name string

Masahiro Kawata

1

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Koichiro Kinoshita

2

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Sumihisa Takahashi

3

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Ken-ichi Ogura

4

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Noriaki Komoto

5

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Mamoru Yamanishi

6

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Takamasa Tobimatsu

7

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Tetsuo Toraya

8

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language of work or name

English

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publication date

29 March 2006

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1 April 2018

Journal of Biological Chemistry

published in

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volume

281

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issue

27

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page(s)

18327-18334

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Radical catalysis in coenzyme B12-dependent isomerization (eliminating) reactions

cites work

1 reference

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Mechanism of hydrogen transfer in the coenzyme B12 dependent dioldehydrase reaction. II

21 January 2018

1 reference

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A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase

21 January 2018

1 reference

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How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex

21 January 2018

1 reference

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Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase

21 January 2018

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Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase

21 January 2018

1 reference

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Coenzyme B12-dependent diol dehydrase: Purification, subunit heterogeneity, and reversible association

21 January 2018

1 reference

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Energetic feasibility of hydrogen abstraction and recombination in coenzyme B(12)-dependent diol dehydratase reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

Understanding the mechanism of B(12)-dependent diol dehydratase: a synergistic retro-push--pull proposal.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

Catalytic roles of active-site amino acid residues of coenzyme B12-dependent diol dehydratase: protonation state of histidine and pull effect of glutamate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

The N-terminal regions of beta and gamma subunits lower the solubility of adenosylcobalamin-dependent diol dehydratase

21 January 2018

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Role of peripheral side chains of vitamin B12 coenzymes in the reaction catalyzed by dioldehydrase

21 January 2018

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Calculation of protein extinction coefficients from amino acid sequence data

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

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Identification of the 1,2-propanediol-1-yl radical as an intermediate in adenosylcobalamin-dependent diol dehydratase reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

Propanediol dehydratase system. Role of monovalent cations in binding of vitamin B12 coenzyme or its analogs to apoenzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

Structure of ribonucleotide reductase protein R1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer

21 January 2018

1 reference

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A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase

21 January 2018

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Inactivation of ribonucleotide reductase by (E)-2'-fluoromethylene-2'-deoxycytidine 5'-diphosphate: a paradigm for nucleotide mechanism-based inhibitors.

21 January 2018

1 reference

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High-field EPR detection of a disulfide radical anion in the reduction of cytidine 5'-diphosphate by the E441Q R1 mutant of Escherichia coli ribonucleotide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601910200

Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M601910200

21 January 2018

Identifiers

DOI

10.1074/JBC.M601910200

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1 April 2018