Amino Acid Sequence of Chicken Liver Glutamate Dehydrogenase

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Glutamate dehydrogenase: amino-acid sequence of the bovine enzyme and comparison with that from chicken liver.

Further investigation of the amino-acid sequence of bovine glutamate dehydrogenase (EC 1.4.1.3) has led to the correction of an earlier tentative sequence. The presently known sequence contains 500 residues in the subunit single peptide chain. The sequence of the homologous enzyme from chicken liver indicates that it contains 503 residues. Of the presently established 485 residues in the chicke...

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Parts of the primary structure of the NAD-specific glutamate dehydrogenase [L-glutamate:NAD oxidoreductase (deaminating), EC 1.4.1.2] from Neurospora crassa are presented. Segments of the sequence representing 886 unique amino-acid residues have been determined; the largest contains 267 residues. There are only short regions of possible homology between this enzyme and the glutamate dehydrogena...

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Amino-acid sequence of NADP-specific glutamate dehydrogenase of neurospora crassa.

A tentative primary structure of the NADP-specific glutamate dehydrogenase [L-glutamate: NADP oxidoreductase (deaminating), EC 1.4.1.4] from Neurospora crassa has been determined. The proposed sequence contains 452 amino-acid residues in each of the identical subunits of the hexameric enzyme. Comparison of the sequence with that of the bovine liver enzyme reveals considerable homology in the am...

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Chicken liver glutamic dehydrogenase.

During the course of fractionation of chicken liver extracts, it was observed that glutamic dehydrogenase could be obtained in the crystalline form after a few simple purification steps. The procedure used in the isolation of glutamic dehydrogenase of chicken liver as well as some of the properties of the crystalline enzyme are described in the present communication. Although the chicken liver ...

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Ox liver glutamate dehydrogenase

1. The effect of pyridoxal 5'-phosphate on the activity of ox liver glutamate dehydrogenase towards different amino acid substrates was investigated. 2. Both alanine and glutamate activities decreased steadily in the presence of pyridoxal 5'phosphate. 3. The alanine/glutamate activity ratio increased as a function of inactivation by pyridoxal 5'-phosphate, indicating that glutamate activity is ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1973

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)44013-1