Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium<i>Salinibacter ruber</i>

Bonete, Marı́a José; Pérez-Pomares, Francisco; Díaz, Susana; Ferrer, Juan Cotino; Oren, Aharon

doi:10.1016/s0378-1097(03)00592-5

Cited by 24 publications

(24 citation statements)

References 23 publications

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“…Interestingly, no inhibitory effect of isophthalate was observed with NAD-GDH from the three strains (Table 1); this is in contrast to bovine NAD-GDH, which is susceptible to inhibition by isophthalate, terephthalate and phthalate (Caughey et al, 1957). The activity of GDH has been reported to be modulated (activation or deactivation) by nucleotides such as ATP, ADP, AMP and GTP (Bonete et al, 2003;LeJohn & Jackson, 1968;Smith et al, 2001Smith et al, , 2002. However, no such modulatory effect was observed with NADP-GDH from the three strains in this study (data not shown).…”

Section: Discussionmentioning

confidence: 47%

“…The induction of NAD-, NADP-or NAD(P)-GDH has also been reported under varying environmental conditions such as salt (Bonete et al, 1990(Bonete et al, , 2003, temperature (Camardella et al, 2002) and nitrogen source (Abrahams & Abratt, 1998;Brown et al, 1973;LeJohn & McCrea, 1968). In Neisseria meningitidis, transcriptional analysis has shown carbon source-dependent expression of gdhA, leading to a difference in the growth of the strain (Pagliarulo et al, 2004).…”

Section: Discussionmentioning

confidence: 94%

“…Depending on the carbon and nitrogen sources, different forms of GDH [NADP-, NAD-or NAD(P)-] have been reported from Clostridium symbiosum (Syed et al, 1991), Laccaria bicolor (Garnier et al, 1997), Escherichia coli (Maurizi & Rasulova, 2002), P. aeruginosa (Smits et al, 1984), Sulfolobus solfataricus (Schinkinger et al, 1991) and Salinibacter ruber (Bonete et al, 2003). The induction of NAD-, NADP-or NAD(P)-GDH has also been reported under varying environmental conditions such as salt (Bonete et al, 1990(Bonete et al, , 2003, temperature (Camardella et al, 2002) and nitrogen source (Abrahams & Abratt, 1998;Brown et al, 1973;LeJohn & McCrea, 1968).…”

Section: Discussionmentioning

confidence: 99%

“…NADP-and NAD-GDH are induced by NH 3 and glutamate, respectively (Hudson & Daniel, 1993;Lu & Abdelal, 2001). The induction of different forms of GDH has been shown in many organisms under conditions such as salt, cold, trophic and environmental stress, and they have been found to be either stable at higher salt concentrations and extreme temperatures, or to have varying affinity for substrates (Bonete et al, 2003;Camardella et al, 2002;Moyano et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

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Carbon source-dependent modulation of NADP-glutamate dehydrogenases in isophthalate-degrading Pseudomonas aeruginosa strain PP4, Pseudomonas strain PPD and Acinetobacter lwoffii strain ISP4

Vamsee-Krishna

Phale

2008

Microbiology

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Acinetobacter lwoffii strain ISP4 metabolizes isophthalate rapidly compared with Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Isophthalate has been reported to be a potent competitive inhibitor of glutamate dehydrogenase (GDH). Exogenous supplementation of isophthalate with glutamate or a-ketoglutarate at 1 mM concentration caused strains PP4 and PPD to grow faster than in the presence of isophthalate alone; however, no such effect was observed in strain ISP4. When grown on isophthalate, all strains showed activity of NADPdependent GDH (NADP-GDH), while cells grown on glucose, 2¾ yeast extract-tryptone broth (2YT) or glutamate showed activities of both NAD-dependent GDH (NAD-GDH) and NADP-GDH. Activity staining, inhibition and thermal stability studies indicated the carbon sourcedependent presence of two (GDH I and GDH II ), three (GDH A , GDH B and GDH C ) and one (GDH P ) forms of NADP-GDH in strains PP4, PPD and ISP4, respectively. The results demonstrate the carbon source-dependent modulation of different forms of NADP-GDH in these bacterial strains. This modulation may help the efficient utilization of isophthalate as a carbon source by overcoming the inhibitory effect on GDH.

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Section: Discussionmentioning

confidence: 47%

Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Carbon source-dependent modulation of NADP-glutamate dehydrogenases in isophthalate-degrading Pseudomonas aeruginosa strain PP4, Pseudomonas strain PPD and Acinetobacter lwoffii strain ISP4

Vamsee-Krishna

Phale

2008

Microbiology

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“…The amination reaction was monitored at the optimum pH using HEPES-NaOH buffer (100 mM, pH 8.0) for all three GDHs; the deamination reaction for GDH I and GDH II was monitored using CAPS-NaOH (100 mM, pH 10), while the deamination reaction for GDH P was monitored using glycine-NaOH (100 mM, pH 9.5). To determine the kinetic constants for the amination reaction, various concentrations of either ␣-KG (0.05 to 50 mM), NH 4 Cl (0.1 to 250 mM), or NADPH (0.0025 to 0.5 mM) and fixed concentrations of other components (5 mM ␣-KG, 200 mM NH 4 Cl, and 0.15 mM NADPH) were used. For the deamination reactions, various concentrations of either glutamate (1 to 500 mM) or NADP (0.0025 to 0.5 mM) and fixed concentration of either NADP (0.2 mM) or glutamate (100 mM for GDH I and GDH P and 200 mM for GDH II ) were used.…”

mentioning

confidence: 99%

Bypassing Isophthalate Inhibition by Modulating Glutamate Dehydrogenase (GDH): Purification and Kinetic Characterization of NADP-GDHs from Isophthalate-Degrading Pseudomonas aeruginosa Strain PP4 and Acinetobacter lwoffii Strain ISP4

Vamsee-Krishna

Phale

2010

J Bacteriol

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Pseudomonas aeruginosa strain PP4 and Acinetobacter lwoffii strain ISP4 metabolize isophthalate as a sole source of carbon and energy. Isophthalate is known to be a competitive inhibitor of glutamate dehydrogenase (GDH), which is involved in C and N metabolism. Strain PP4 showed carbon source-dependent modulation of NADP-GDH; GDH I was produced when cells were grown on isophthalate, while GDH II was produced when cells were grown on glucose. Strain ISP4 produced a single form of NADP-GDH, GDH P , when it was grown on either isophthalate or rich medium (2YT). All of the forms of GDH were purified to homogeneity and characterized. GDH I and GDH II were found to be homotetramers, while GDH P was found to be a homohexamer. GDH II was more sensitive to inhibition by isophthalate (2.5-and 5.5-fold more sensitive for amination and deamination reactions, respectively) than GDH I . Differences in the N-terminal sequences and electrophoretic mobilities in an activity-staining gel confirmed the presence of two forms of GDH, GDH I and GDH II , in strain PP4. In strain ISP4, irrespective of the carbon source, the GDH P produced showed similar levels of inhibition with isophthalate. However, the specific activity of GDH P from isophthalate-grown cells was 2.5-to 3-fold higher than that of GDH P from 2YT-grown cells. Identical N-terminal sequences and electrophoretic mobilities in the activity-staining gel suggested the presence of a single form of GDH P in strain ISP4. These results demonstrate the ability of organisms to modulate GDH either by producing an entirely different form or by increasing the level of the enzyme, thus enabling strains to utilize isophthalate more efficiently as a sole source of carbon and energy.Phthalate isomers and their esters are used widely in various industries and are considered potent pollutants because of their carcinogenic, mutagenic, teratogenic, and endocrine-disrupting properties (31, 32). Due to the persistence of these compounds in the environment, microorganisms have evolved and adapted to utilize them as sole sources of carbon and energy. 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).Pseudomonas aeruginosa strain PP4 and Acinetobacter lwoffii strain ISP4 utilize isophthalate as a sole source of carbon and energy (31, 32). Thus, in these strains, the carbo...

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Salinibacter

Antón¹,

Amann²,

Rosselló‐Móra³

2015

Bergey's Manual of Systematics of Archaea and Bacteria

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Sa.li.ni.bac'ter. L. fem. pl. n. salinae salterns, salt‐works; N.L. masc. n. bacter masc. equivalent of the Gr. neut. n. baktron a rod; N.L. masc. n. Salinibacter a rod from salt‐works. Bacteroidetes / Cytophagia / Incertae sedis II / Rhodothermaceae / Salinibacter Rod‐shaped , often slightly curved. Gram‐stain‐negative. Motile by means of flagella. Obligately aerobic . Catalase‐ and oxidase‐positive. Nitrate is not reduced. Extremely halophilic , requiring at least 15% NaCl (w/v) to grow; optimum, 20–30%. Chemoheterotrophic. Grows best at low substrate concentrations; high levels of organic compounds may be inhibitory. Amino acids are the preferred substrates for growth. Salinibacter strains form a deep branch of the phylum Bacteroidetes of the domain Bacteria . Colonies are bright red/orange ‐pigmented. Among the most salt‐tolerant and salt‐requiring strains within the bacterial domain. DNA G + C content ( mol %): 66.3–67.7 (HPLC). Type species : Salinibacter ruber Antón, Oren, Benlloch, Rodríguez‐Valera, Amann and Rosselló‐Mora 2002, 490 VP .

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Occurrence of two different glutamate dehydrogenase activities in the halophilic bacteriumSalinibacter ruber

Cited by 24 publications

References 23 publications

Carbon source-dependent modulation of NADP-glutamate dehydrogenases in isophthalate-degrading Pseudomonas aeruginosa strain PP4, Pseudomonas strain PPD and Acinetobacter lwoffii strain ISP4

Carbon source-dependent modulation of NADP-glutamate dehydrogenases in isophthalate-degrading Pseudomonas aeruginosa strain PP4, Pseudomonas strain PPD and Acinetobacter lwoffii strain ISP4

Bypassing Isophthalate Inhibition by Modulating Glutamate Dehydrogenase (GDH): Purification and Kinetic Characterization of NADP-GDHs from Isophthalate-Degrading Pseudomonas aeruginosa Strain PP4 and Acinetobacter lwoffii Strain ISP4

Salinibacter

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