Amino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum-Reference-Cited by-同舟云学术

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Amino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum

Published:1999-02 Issue:3 Volume:1426 Page:513-525
ISSN:0304-4165
Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Pérez-Pomares Francisco,Ferrer Juan,Camacho Mónica,Pire Carmen,LLorca Francisco,Bonete Marı&#x;aJosé

Funder

Generalitat Valenciana

Comisión Interministerial de Ciencia y Tecnología

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference33 articles.

1. E.L. Smith, B.M. Austen, K.M. Blumenthal, J.F. Nyc, in: P.D. Boyer (Ed.), The Enzymes vol. XI, Academic Press, New York, 1975, pp. 294–366.

2. The essentail active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phophate

3. Subunit assembly and active site location in the structure of glutamate dehydrogenase

4. Bovine liver glutamate dehydrogenase. Equilibriums and kinetics of inactivation by pyridoxal

5. The reaction of a histidine residue in glutamate dehydrogenase with diethyl pyrocarbonate

Cited by 8 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Residues His172 and Lys238 are Essential for the Catalytic Activity of the Maleylacetate Reductase from Sphingobium chlorophenolicum Strain L-1;Scientific Reports;2017-12

2. Recent Advances in the Nitrogen Metabolism in Haloarchaea and Its Biotechnological Applications;Biotechnology of Extremophiles:;2016

3. Metabolism of halophilic archaea;Extremophiles;2008-02-16

4. Gene cloning, heterologous overexpression and optimized refolding of the NAD-glutamate dehydrogenase from Haloferax mediterranei;Extremophiles;2005-10-01

5. Occurrence of two different glutamate dehydrogenase activities in the halophilic bacteriumSalinibacter ruber;FEMS Microbiology Letters;2003-09

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