Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.4.1.2 (glutamate dehydrogenase)
4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem J. (1975) 145, 5.
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PMID:The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides. 0 Oct

The extracellular proteinase of Staphylococcus aureus strain V8 was used to digest the NADP-specific glutamate dehydrogenase of Neurospora crassa. Of 35 non-overlapping peptides expected from the glutamate content of the polypeptide chain, 29 were isolated and substantially sequenced. The sequences obtained were valuable in providing overlaps for the alignment of about two-thirds of the sequences found in tryptic peptides [Wootton, J. C., Taylor, J, G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 739-748]. The blocked N-terminal peptide of the protein was isolated. This peptide was sequenced by mass spectrometry, and found to have N-terminal N-acetylserine by Howard R. Morris and Anne Dell, whose results are presented as an Appendix to the main paper. The staphylococcal proteinase showed very high specificity for glutamyl bonds in the NH4HCO3 buffer used. Partial splits of two aspartyl bonds, both Asp-Ile, were probably attributable to the proteinase. No cleavage of glutaminyl or S-carboxymethylcysteinyl bonds was found. Additional experimental detail has been deposited as Supplementary Publication SUP 50053 (5 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K, from whom copies may be obtained under the terms given in Biochem. J. (1975) 1458 5.
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PMID:The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptides from digestion with a staphylococcal proteinase. 0 Oct 1

Peptic and chymotryptic peptides were isolated form the NADP-specific glutamate dehydrogenase of Neurospora crassa and substantially sequenced. Out of 452 residues in the polypeptide chain, 265 were recovered in the peptic and 427 in the chymotryptic peptides. Together with the tryptic peptides [Wootton, J. C., Taylor, J. G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 749-755], these establish the complete sequence of the chain, including the acid and amide assignments, except for seven places where overlaps are inadequate. These remaining alignments are deduced from information on the CNBr fragments obtained in another laboratory [Blumenthal, K. M., Moon, K. & Smith, E. L. (1975), J. Biol. Chem. 250, 3644-3654]. Further information has been deposited as Supplementary Publication SUP 50054 (17 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem. J. (1975) 145, 5.
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PMID:The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence. 0 Oct 2

The kinetic properties of the constitutive double specific glutamate dehydrogenase (NAD(P)--GDH) and the inducible NADP-specific glutamate dehydrogenase (NADP--GDH) of Chlorella pyrenoidosa Pringsheim 82T (thermophilic strain) in a deaminating reaction have been studied. NAD(P)-GDH behaves in a deamination as a Michaelis-Menten enzyme. NADP-GDH displays some lag-period before a steady-state phase. The duration of this lag depends on a substrate concentration. Besides that, an effect of all the substrates on a heat inactivation of both GDH and a product inhibition have been studied. All the substrates except the reduced co-factors protect effectively GDH from the heat inactivation, especially the thermolabille NADP-GDH. On the contrary, NAD(P)-H promote the heat inactivation of both GDH. The product inhibition analysis shows that the inducible NADP-GDH acts in vivo as a synthetic enzyme. In the previous paper (V. R. Shatilov et all., 1974, Dokl. Acad. Nauk USSR, 216,223) it was shown for the constitutive GDH that p-CMB strongly inhibited a desamination and slightly (if any) affect an amination. It this paper it is shown that action of p-CMB on the amination depends on the presence of NAD+ (not NADP+ or L-glutamate). p-CMB and NAD+ affect tha amination in a strongly sunergetic manner. Some suggestions about the intracellular localization of chlorella GDH are made.
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PMID:[Comparative study of glutamate dehydrogenases of Chlorella]. 0 35

1. NADP-dependent glutamate dehydrogenase (EC 1.4.1.4) extracted from nuclear fractions of Saccharomyces cerevisiae was partially purified. The final purification achieved was over 100-fold over the initial extract. 2. Cellulose acetate electrophoresis shows that the preparation is close to homogeneity and that the enzyme is slightly more anionic than cytoplasmic glutamate dehydrogenase. 3. The response of the nuclear activity to variation of pH, of inorganic phosphate and other electrolyte concentration and of the concentration of the reaction substrates has been investigated. Several differences were detected in comparison with cytoplasmic glutamate dehydrogenase.
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PMID:Purification and properties of NADP-dependent glutamate dehydrogenase from yeast nuclear fractions. 0 26

Biotin deficiency in Aspergillus nidulans has been found to increase the uptake of ammonium ions, associated with a marked increase in the activity of NADP-linked glutamate dehydrogenase, which is found to be the major route of ammonia assimilation in this culture. The results obtained are discussed with respect to the growth of Aspergillus nidulans during biotin deficiency.
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PMID:Assimilation of ammonia and growth of biotin deficient Aspergillus nidulans. 0 83

The NADP-specific glutamate dehydrogenase (EC 1.4.1.4) of Neurospora crassa is inhibited by reaction with 1,2-cyclohexanedione which binds to arginine residues. With the 14C-labeled reagent, a peptide was isolated with the sequence: Gly-Gly-Leu-Arg-Leu-His-Pro-Ser-Val-Asn-Leu, corresponding to residues 78 through 88 in the protein. The arginine, residue 81, was present as N7,N8-(1,2-dihydroxycyclohex-1,2-ylene)-arginyl (or DHCH-arginine). Present evidence indicates that this arginine residue resides at or near the nicotinamide binding domain of the enzyme. Similar sequences are present in the bovine liver enzyme (EC 1.4.1.3) and the NAD-specific glutamate dehydrogenase of Neurospora (EC 1.4.1.2).
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PMID:Identification of a functional arginine residue involved in coenzyme binding by the NADP-specific glutamate dehydrogenase of Neurospora. 0 4

NH+4 excretion was undetectable in N2-fixing cultures of Rhodospirillum rubrum (S-1) and nitrogenase activity in these cultures was repressed by the addition of 10 mM NH+4 to the medium. The glutamate analog, L-methionine-DL-sulfoximine (MSX), derepressed N2 fixation even in the presence of 10 mM extracellular NH+4. When 10 mg MSX/ml was added to cultures just prior to nitrogenase induction they developed nitrogenase activity (20% of the control activities) and excreted most of their fixed N2 as NH+4. Nitrogenase activities and NH+4 production from fixed N2 were increased considerably when a combined nitrogen source, NH+4 (greater than 40 mumoles NH+4/mg cell protein in 6 days) or L-glutamate (greater than 60 mumoles NH+4/ mg cell protein in 6 days) was added to the cultures together with MSX. Biochemical analysis revealed that R. rubrum produced glutamine synthetase and glutamate synthase (NADP-dependent) but no detectable NADP-dependent glutamate dehydrogenase. The specific activity of glutamine synthetase was observed to be maximal when nitrogenase activity was also maximal. Nitrogenase and glutamine synthetase activities were repressed by NH+4 as well as by glutamate. The results demonstrate that utilization of solar energy to photoproduce large quantities of NH+4 from N2 is possible with photosynthetic bacteria by interfering with their regulatory control of N2 fixation.
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PMID:Photoproduction of ammonium ion from N2 in Rhodospirillum rubrum. 1 53

Kinetic analyses done with cell-free extracts of this basidiomycete fungus showed that the NADP-linked glutamate dehydrogenase exhibited positively co-operative interactions with the substrates 2-oxoglutarate and NADPH, negatively co-operative kinetics with NADP+ and was extremely sensitive to inhibition of deamination activity by ammonium and/or ammonia. The NAD-linked enzyme showed positive co-operativity with NADH, Michaelis-Menten kinetics with all other substrates and was subject only to mild inhibitions by the reaction products. Considered together with the values of the Michaelis constants, these results indicate that the former enzyme is primarily concerned with the amination of 2-oxoglutarate when the concentration of this substrate exceeds about 4 mM, while the NAD-linked enzyme is able to aminate or deaminate as metabolic conditions require. Synthesis of both enzymes was repressed by addition of carbamyl phosphate or N-acetyl-glutamate to mycelial cultures growing in media containing glucose and ammonium as carbon and nitrogen sources. Growth in media containing urea results in repression of the NADP-linked glutamate dehydrogenase and derepression of the NAD-linked enzyme. Such results indicate a connexion between the glutamate dehydrogenases and the urea cycle. It is suggested that under normal conditions of growth on complex media nitrogen is assimilated in the form of amino acids and that the glutamate dehydrogenases act in support of transaminases to allow this process to continue, and in support of the urea cycle to allow the disposal of excess nitrogen.
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PMID:Factors affecting the amount and the activity of the glutamate dehydrogenases of Coprinus cinereus. 1 62

Bacillus subtilis PCI 219 has a single glutamate dehydrogenase (GDH) [EC 1.4.1.3] with dual coenzyme specificity [for NAD(H) and NADP(H)]. The enzyme was purified 800-fold from crude extracts of B. subtilis from the post-exponential phase of growth and showed one significant protein band on gel electrophoresis. This band was determined, by activity staining, to have all the GDH nucleotide specificities. Its molecular weight was estimated to be 250,000+/-20,000 by gel filtration, and 270,000+/-30,000 by zone centrifugation in a sucrose density gradient. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate showed that GDH has a subunit size of about 57,000. The pI of GDH was found to bepH 3.7 by isoelectric focusing. GDH exhibited nonlinear kinetics in the reduction of NAD+, and in the reverse direction, the substrate, NH4+, was strongly inhibitory at high concentrations. Purine nucleotides did not affect the activity. The oxidative demination of glutamate was significantly inhibited by the metabolites oxaloacetate and citrate, which acted as allosteric effectors of this enzyme,inhibiting the reaction in one direction. The pH optimum of each of the activities of GDH and the stability of GDH are also reported.
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PMID:Glutamate dehydrogenase from Bacillus subtilis PCI 219. I. Purification and properties. 1 49


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