The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.

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Measurement of key metabolic enzyme activities in mammalian cells using rapid and sensitive microplate-based assays.

P2860

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P2860

The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.

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http://www.wikidata.org/entity/Q41821061

description

1984 nî lūn-bûn

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1984年の論文

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1984年論文

@yue

1984年論文

@zh-hant

1984年論文

@zh-hk

1984年論文

@zh-mo

1984年論文

@zh-tw

1984年论文

@wuu

1984年论文

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1984年论文

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name

The kinetic mechanism of ox li ...... ve deamination of L-glutamate.

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type

Item

label

The kinetic mechanism of ox li ...... ve deamination of L-glutamate.

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The kinetic mechanism of ox li ...... ve deamination of L-glutamate.

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P1476

The kinetic mechanism of ox li ...... ve deamination of L-glutamate.

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P2093

Aitchison MJ

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Engel PC

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Hornby DP

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P2860

Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme

Effects of adenosine 5'-diphosphate on bovine glutamate dehydrogenase: diethyl pyrocarbonate modification

Glutamic dehydrogenase. II. The effect of various nucleotides on the association-dissociation and kinetic properties.

Dynamic aspects of enzyme specificity.

The preparation of pure salt-free nicotinamide coenzymes.

Ox liver glutamate dehydrogenase. The role of lysine-126 reappraised in the light of studies of inhibition and inactivation by pyridoxal 5'-phosphate.

A product-inhibition study of bovine liver glutamate dehydrogenase.

The allosteric mechanism of bovine liver glutamate dehydrogenase. Evidence from circular-dichroism studies for a conformational change in the ternary complex enzyme-(oxidized nicotinamide-adenine dinucleotide)-glutarate.

Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate.

The significance of abrupt transitions in Lineweaver-Burk plots with particular reference to glutamate dehydrogenase. Negative and positive co-operativity in catalytic rate constants.

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161-168

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scholarly article

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10.1042/BJ2230161

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English

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223

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1984-10-01T00:00:00Z

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17036062

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6149744

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1144276

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The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.

about

P2860

P2860

The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.

description

name

type

label

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

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P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932