2007
DOI: 10.1016/j.febslet.2007.05.032
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Competitive inhibition of glutamate dehydrogenase reaction

Abstract: Irrespective of their pyridine nucleotide specificity, all glutamate dehydrogenases share a common chemical mechanism that involves an enzyme bound 'iminoglutarate' intermediate. Three compounds, structurally related to this intermediate, were tested for the inhibition of purified NADP-glutamate dehydrogenases from two Aspergilli, as also the bovine liver NAD(P)-glutamate dehydrogenase. 2-Methyleneglutarate, closely resembling iminoglutarate, was a potent competitive inhibitor of the glutamate dehydrogenase re… Show more

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Cited by 22 publications
(15 citation statements)
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“…These concentrations are in the same range of those observed for the same assay in other organisms, such as Synechocystis PCC 6803 (Florencio et al. , 1987; Chávez and Candau, 1991), Aspergilllus niger (Choudhury and Punekar, 2007) and Klebsiella pneumoniae (Kim et al. , 2002).…”
Section: Resultssupporting
confidence: 76%
“…These concentrations are in the same range of those observed for the same assay in other organisms, such as Synechocystis PCC 6803 (Florencio et al. , 1987; Chávez and Candau, 1991), Aspergilllus niger (Choudhury and Punekar, 2007) and Klebsiella pneumoniae (Kim et al. , 2002).…”
Section: Resultssupporting
confidence: 76%
“…2 the coenzyme specificity, GDHs can be classified as (a) NADP + -dependent, (b) NAD + -dependent, and (c) NAD + /NADP + -dependent (or dual specific) (6)(7)(8). Generally, the GDHs involved in ammonium assimilation are NADP + -specific, whereas the NAD + -dependent enzymes are involved in glutamate catabolism (9).…”
Section: Structural Insights Into the Catalytic Properties Of Gdhmentioning
confidence: 99%
“…Interestingly, GDHs from strains PP4 and ISP4 showed a mixed partial type of inhibition with isophthalate, suggesting that isophthalate binds not only to the enzyme form but also to the enzyme-substrate form. The inhibition constants (K i ) with isophthalate suggested that deamination reactions were far more sensitive to inhibition than amination reactions, as observed with several GDHs (5,13,16,27,28,30,34). The K i values suggested that compared to GDH I , GDH II has a higher affinity for isophthalate, thus making it more susceptible to inhibition.…”
Section: Discussionmentioning
confidence: 99%
“…Compared to the organisms whose metabolic pathways for isophthalate degradation have been studied, a large number of organisms have been studied in detail to determine their metabolic pathways for phthalate and terephthalate degradation (12,17,18,20,25,26,29,31,32,35,36). The fewer isophthalate-degrading strains and the difficulties in isolating them could be due to the fact that isophthalate acts as a competitive inhibitor of glutamate dehydrogenase (GDH), which plays an important role at the interface of C metabolism and N metabolism (5,11,13,16,27,28,30,33,34). GDH performs oxidative deamination of glutamate to ␣-ketoglutarate (␣-KG) and reductive amination of ␣-KG to glutamate, and depending on the cofactor requirement the enzyme is either NAD-, NADP-, or NAD(P)-GDH (7,19).…”
mentioning
confidence: 99%