5 Glutamate Dehydrogenases

Smith, Emil L.; Austen, Brian; Blumenthal, Kenneth M.; Nyc, Joseph F.

doi:10.1016/s1874-6047(08)60213-9

Cited by 235 publications

(218 citation statements)

References 220 publications

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“…We used the published amino acid sequence information of human, bovine, rat, and chicken liver GLUD (1,14) to synthesize oligonucleotide probes corresponding to regions of low redundancy and high interspecies homology. The (18).…”

Section: Methodsmentioning

confidence: 99%

“…), a mitochondrial enzyme, is known to catalyze the reversible oxidative deamination of L-glutamate to a-ketoglutarate using NAD and/or NADP as cofactors (1). The enzyme links the L-amino acids with the Krebs cycle, which provides a major pathway for the metabolic interconversion of a-amino acids and a-keto acids.…”

mentioning

confidence: 99%

“…The enzyme links the L-amino acids with the Krebs cycle, which provides a major pathway for the metabolic interconversion of a-amino acids and a-keto acids. Substantial amounts of GLUD activity are known to be present in different mammalian organs such as liver and brain and in leukocytes (1,2). Evidence has been accumulated in recent years to suggest that GLUD is of importance in the biology of the nervous tissue and the pathogenesis of human neurodegenerative disorders (2,3).…”

mentioning

confidence: 99%

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Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family.

Mavrothalassitis

Tzimagiorgis

Mitsialis

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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We have isolated a series of human liver cDNA clones encoding glutamate dehydrogenase. The cDNAderived protein sequence specifies a single 558-amino acid long polypeptide including a cleavable signal sequence of 53 amino acids. Blotting analysis of RNA from human, monkey, and rabbit showed that glutamate dehydrogenase mRNA is present in various amounts in all tissues tested. Glutamate dehydrogenase mRNAs are of four sizes and are found in different ratios in different tissues; the predominant ones are ".3.5 and =2.9 kilobases. Blot hybridization of human genomic DNA to nonoverlapping cDNA fragments revealed multiple bands, many of which hybridize with two or more probes in a manner inconsistent with the existence of a single GLUD gene. Moreover, two separate 36-base synthetic oligonucleotides corresponding to the coding region hybridize to multiple genomic fragments, confirming the existence of more than one GLUDrelated gene in human.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family.

Mavrothalassitis

Tzimagiorgis

Mitsialis

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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“…In addition to ammonia and the respective 2-oxocarboxylic acid, amino acid dehydrogenases need a cosubstrate, which supplies the hydride ions for the reduction of the intermediate Schiff bases. [22] For example, nicotinamide adenine dinucleotide (NADH) is a suitable cosubstrate. The oxidized cosubstrates (e.g.…”

Section: Amino Acid Dehydrogenasesmentioning

confidence: 99%

“…l-Lysine (19) enters the cells with the assistance of the overexpressed l-lysine permease transport system and is there deaminated to the aldehyde-amino acid 21 by the lysine aminotransferase from Flavobacterium lutescens. Amino acid 21 is in equilibrium with 2,3,4,5-tetrahydropyridine-2-carboxylic acid (22) and is reduced to (S)-20 with the intrinsic pyrroline-5-carboxylate reductase of E. coli and NADPH. [26] The conversion observed is greater than 90 % with respect to l-lysine, and (S)-20 is obtained from the culture filtrate in 70 % yield after purification.…”

Section: Aminotransferasesmentioning

confidence: 99%

Industrial Methods for the Production of Optically Active Intermediates

Breuer¹,

Ditrich²,

Habicher³

et al. 2004

Angew Chem Int Ed

1,316

625

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Enantiomerically pure amino acids, amino alcohols, amines, alcohols, and epoxides play an increasingly important role as intermediates in the pharmaceutical industry and agrochemistry, where both a high degree of purity and large quantities of the compounds are required. The chemical industry has primarily relied upon established chemical methods for the synthesis of these intermediates, but is now turning more and more to enzymatic and biotechnological fermentation processes. For the industrial implementation of many transformations alternative methods are available. The advantages of the individual methods will be discussed herein and exemplified by syntheses of relevant compounds.

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Activity of glutamate dehydrogenase is increased in ammonia‐stressed hybridoma cells

Bonarius¹,

Houtman²,

Gooijer³

et al. 1998

Biotechnol. Bioeng.

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The effect of added ammonia on the intracellular fluxes in hybridoma cells was investigated by metabolic-flux balancing techniques. It was found that, in ammonia-stressed hybridoma cells, the glutamate-dehydrogenase flux is in the reverse direction compared to control cells. This demonstrates that hybridoma cells are able to prevent the accumulation of ammonia by converting ammonia and alpha-ketoglutarate into glutamate. The additional glutamate that is produced by this flux, as compared to the control culture, is converted by the reactions catalyzed by alanine aminotransferase (45% of the extra glutamate) and aspartate aminotransferase (37%), and a small amount is used for the biosynthesis of proline (6%). The remaining 12% of the extra glutamate is secreted into the culture medium. The data suggest that glutamate dehydrogenase is a potential target for metabolic engineering to prevent ammonia accumulation in high-cell-density culture.

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5 Glutamate Dehydrogenases

Cited by 235 publications

References 220 publications

Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family.

Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family.

Industrial Methods for the Production of Optically Active Intermediates

Activity of glutamate dehydrogenase is increased in ammonia‐stressed hybridoma cells

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