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 α-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 NADP-dependent GDH (NADP-GDH), while cells grown on glucose, 2× 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 source-dependent presence of two (GDHI and GDHII), three (GDHA, GDHB and GDHC) and one (GDHP) 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.
AbrahamsG. L.,
AbrattV. R.1998; The NADH-dependent glutamate dehydrogenase enzyme of Bacteroides fragilis Bf1 is induced by peptides in the growth medium. Microbiology 144:1659–1667
BoneteM. J.,
Perez-PomaresF.,
DiazS.,
FerrerJ.,
OrenA.2003; Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber
. FEMS Microbiol Lett 226:181–186
BradfordM. M.1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
CamardellaL.,
Di FraiaR.,
AntignaniA.,
CiardielloM. A.,
di PriscoG.,
ColemanJ. K.,
BuchonL.,
GuespinJ.,
RussellN. J.2002; The Antarctic Psychrobacter sp. TAD1 has two cold-active glutamate dehydrogenases with different cofactor specificities. Characterisation of the NAD+-dependent enzyme. Comp Biochem Physiol A Mol Integr Physiol 131:559–567
CunliffeD.,
LeasonM.,
ParkinD.,
LeaP. J.1983; The inhibition of glutamate dehydrogenase by derivatives of isophthalic acid. Phytochemistry 22:1357–1360
GarnierA.,
BerredjemA.,
BottonB.1997; Purification and characterization of the NAD-dependent glutamate dehydrogenase in the ectomycorrhizal fungus Laccaria bicolor (Maire) orton. Fungal Genet Biol 22:168–176
JaegerR. J.,
RubinR. J.1973; Extraction, localization, and metabolism of di-2-ethylhexyl phthalate from PVC plastic medical devices. Environ Health Perspect 3:95–102
KochH. M.,
DrexlerH.,
AngererJ.2003; An estimation of the daily intake of di(2-ethylhexyl)phthalate (DEHP) and other phthalates in the general population. Int J Hyg Environ Health 206:77–83
LeJohnH. B.,
JacksonS.1968; Allosteric interactions of a regulatory nicotinamide adenine dinucleotide-specific glutamate dehydrogenase from Blastocladiella. A molecular model for the enzyme. J Biol Chem 243:3447–3457
LuC. D.,
AbdelalA. T.2001; The gdhB gene of Pseudomonas aeruginosa encodes an arginine-inducible NAD+-dependent glutamate dehydrogenase which is subject to allosteric regulation. J Bacteriol 183:490–499
MauriziM. R.,
RasulovaF.2002; Degradation of l-glutamate dehydrogenase from Escherichia coli: allosteric regulation of enzyme stability. Arch Biochem Biophys 397:206–216
MoyanoE.,
CardenasJ.,
Muñoz-BlancoJ.1992; Purification and properties of three NAD(P)+ isozymes of l-glutamate dehydrogenase of Chlamydomonas reinhardtii
. Biochim Biophys Acta111963–68
NoorS.,
PunekarN. S.2005; Allosteric NADP-glutamate dehydrogenase from aspergilli: purification, characterization and implications for metabolic regulation at the carbon–nitrogen interface. Microbiology 151:1409–1419
RubinR. J.,
JaegerR. J.1973; Some pharmacologic and toxicologic effects of di-2-ethylhexyl phthalate (DEHP) and other plasticizers. Environ Health Perspect 3:53–59
SchinkingerM. F.,
RedlB.,
StofflerG.1991; Purification and properties of an extreme thermostable glutamate dehydrogenase from the archaebacterium Sulfolobus solfataricus
. Biochim Biophys Acta 1073:142–148
SchlafliH. R.,
WeissM. A.,
LeisingerT.,
CookA. M.1994; Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component. J Bacteriol 176:6644–6652
SmithT. J.,
SchmidtT.,
FangJ.,
WuJ.,
SiuzdakG.,
StanleyC. A.2002; The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol 318:765–777
SmitsR. A.,
PieperF. R.,
van der DriftC.1984; Purification of NADP-dependent glutamate dehydrogenase from Pseudomonas aeruginosa and immunochemical characterization of its in vivo inactivation. Biochim Biophys Acta 801:32–39
StevensL.,
DuncanD.,
RobertsonP.1989; Purification and characterisation of NAD-glutamate dehydrogenase from Aspergillus nidulans
. FEMS Microbiol Lett 48:173–177
SyedS. E.,
EngelP. C.,
ParkerD. M.1991; Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD+-dependent glutamate dehydrogenase of Clostridium symbiosum
. Biochim Biophys Acta1115123–130
TarasevM.,
BallouD. P.2005; Chemistry of the catalytic conversion of phthalate into its cis-dihydrodiol during the reaction of oxygen with the reduced form of phthalate dioxygenase. Biochemistry 44:6197–6207
WangY. Z.,
ZhouY.,
ZylstraG. J.1995; Molecular analysis of isophthalate and terephthalate degradation by Comamonas testosteroni YZW-D. Environ Health Perspect 103:9–12
WangY.,
FanY.,
GuJ. D.2003; Microbial degradation of the endocrine-disrupting chemicals phthalic acid and dimethyl phthalate ester under aerobic conditions. Bull Environ Contam Toxicol 71:810–818