Mechanistic and active-site studies on D(--)-mandelate dehydrogenase from Rhodotorula graminis.

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http://www.wikidata.org/entity/Q41838304

description

1992 nî lūn-bûn

@nan

1992年の論文

@ja

1992年論文

@yue

1992年論文

@zh-hant

1992年論文

@zh-hk

1992年論文

@zh-mo

1992年論文

@zh-tw

1992年论文

@wuu

1992年论文

@zh

1992年论文

@zh-cn

name

Mechanistic and active-site st ...... ase from Rhodotorula graminis.

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type

Item

label

Mechanistic and active-site st ...... ase from Rhodotorula graminis.

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prefLabel

Mechanistic and active-site st ...... ase from Rhodotorula graminis.

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P1476

Mechanistic and active-site st ...... ase from Rhodotorula graminis.

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P2093

Baker DP

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Fewson CA

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Keen JN

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Kleanthous C

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Weinhold E

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

From analysis to synthesis: new ligand binding sites on the lactate dehydrogenase framework. Part I.

Microbial metabolism of mandelate: a microcosm of diversity.

Determination of the hydride transfer stereospecificity of nicotinamide adenine dinucleotide linked oxidoreductases by proton magnetic resonance.

Stereospecificities of the pyridine nucleotide-linked enzymes.

Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli.

Archaebacterial malate dehydrogenases. The enzymes from the thermoacidophilic organisms Sulfolobus acidocaldarius and Thermoplasma acidophilum show A-side stereospecificity for NAD+.

3-(Bromoacetyl)chloramphenicol, an active site directed inhibitor for chloramphenicol acetyltransferase.

Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with a radiolabeled bifunctional arsenoxide: evidence for an essential histidine residue at the active site of lipoamide dehydrogenase.

An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase.

P304

211-218

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P31

scholarly article

P356

10.1042/BJ2810211

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P407

English

P478

281 ( Pt 1)

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P577

1992-01-01T00:00:00Z

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P5875

21423546

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P698

1731758

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P921

(R)-mandelate dehydrogenase activity

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1130663

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