Mechanistic Characterization of Escherichia coli l-Aspartate Oxidase from Kinetic Isotope Effects.

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Mechanistic Characterization of Escherichia coli l-Aspartate Oxidase from Kinetic Isotope Effects.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

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2017年論文

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Mechanistic Characterization o ...... from Kinetic Isotope Effects.

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Mechanistic Characterization o ...... from Kinetic Isotope Effects.

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Mechanistic Characterization o ...... from Kinetic Isotope Effects.

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P1476

Mechanistic Characterization o ...... from Kinetic Isotope Effects.

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P2093

Carmen Chow

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Subray Hegde

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P2860

Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B

Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family

The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation

Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis

The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation

Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 A resolution

On the catalytic mechanism of choline oxidase

D-aspartate oxidase of kidney.

L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.

Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations.

P304

4044-4052

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scholarly article

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10.1021/ACS.BIOCHEM.7B00307

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English

P433

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P478

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P50

John S Blanchard

P577

2017-07-26T00:00:00Z

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P698

28700220

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P932

5839506

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