(Q27676576)

English

Redesign of coenzyme B(12) dependent diol dehydratase to be resistant to the mechanism-based inactivation by glycerol and act on longer chain 1,2-diols

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scholarly article

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Redesign of coenzyme B(12) dependent diol dehydratase to be resistant to the mechanism-based inactivation by glycerol and act on longer chain 1,2-diols (English)

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author name string

Mamoru Yamanishi

1

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Koichiro Kinoshita

2

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Masaki Fukuoka

3

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Takuya Saito

4

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Aya Tanokuchi

5

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Yuuki Ikeda

6

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Hirokazu Obayashi

7

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Koichi Mori

8

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Naoki Shibata

9

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Takamasa Tobimatsu

10

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Tetsuo Toraya

11

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language of work or name

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publication date

March 2012

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279

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5

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793-804

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

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Resolutin of the coenzyme B-12-independent dehydratases of Klebsiella sp. and Citrobacter freundii

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Mechanism of action of adenosylcobalamin: glycerol and other substrate analogs as substrates and inactivators for propanediol dehydratase - kinetics, stereospecificity, and mechanism

1 reference

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Study of the mechanism of action of adenosylcobalamindependent glycerol dehydratase from Aerobacter aerogenes. II. The inactivation kinetics of glycerol dehydratase complexes with adenosylobalamin and its analogs

1 reference

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Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase

1 reference

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Characterization and mechanism of action of a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase

1 reference

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Identification and expression of the genes and purification and characterization of the gene products involved in reactivation of coenzyme B12-dependent glycerol dehydratase of Citrobacter freundii

1 reference

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Molecular basis for specificities of reactivating factors for adenosylcobalamin-dependent diol and glycerol dehydratases

1 reference

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Diol dehydratase-reactivating factor is a reactivase--evidence for multiple turnovers and subunit swapping with diol dehydratase

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

1 reference

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

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

1 reference

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Coenzyme B12-dependent diol dehydratase is a potassium ion-requiring calcium metalloenzyme: evidence that the substrate-coordinated metal ion is calcium

1 reference

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The crystal structure of coenzyme B12-dependent glycerol dehydratase in complex with cobalamin and propane-1,2-diol

1 reference

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

1 reference

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Relative enantiomer binding and reaction rates with propanediol dehydrase

1 reference

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Processing of X-ray diffraction data collected in oscillation mode

1 reference

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The CCP4 suite: programs for protein crystallography

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Version 1.2 of the Crystallography and NMR system

1 reference

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Coot: model-building tools for molecular graphics

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MolProbity: all-atom structure validation for macromolecular crystallography

1 reference

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

1 reference

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

1 reference

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Klebsiella pneumoniae 1,3-propanediol:NAD+ oxidoreductase

1 reference

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Calculation of protein extinction coefficients from amino acid sequence data

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DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS

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

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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UCSF Chimera--a visualization system for exploratory research and analysis

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Identifiers

10.1111/J.1742-4658.2012.08470.X

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