Involvement of an arginine residue in glutamate dehydrogenase with the 1-position carboxyl of glutamate

LEE JANSON; ELLIS BELL

doi:10.1042/bst0160860

Involvement of an arginine residue in glutamate dehydrogenase with the 1-position carboxyl of glutamate

Biochemical Society Transactions ◽

10.1042/bst0160860 ◽

1988 ◽

Vol 16 (5) ◽

pp. 860-861

Author(s):

LEE JANSON ◽

ELLIS BELL

Keyword(s):

Glutamate Dehydrogenase ◽

Arginine Residue

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Identification of a functional arginine residue involved in coenzyme binding by the NADP-specific glutamate dehydrogenase of Neurospora.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)33134-4 ◽

1976 ◽

Vol 251 (18) ◽

pp. 5835-5837

Author(s):

B M Austen ◽

E L Smith

Keyword(s):

Glutamate Dehydrogenase ◽

Arginine Residue ◽

Coenzyme Binding

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Inactivation of glutamate dehydrogenase and glutamate synthase from Bacillus megaterium by phenylglyoxal, butane-2,3-dione and pyridoxal 5′-phosphate

Biochemical Journal ◽

10.1042/bj1730053 ◽

1978 ◽

Vol 173 (1) ◽

pp. 53-58 ◽

Cited By ~ 4

Author(s):

I A Hemmilä ◽

P I Mäntsälä

Keyword(s):

Enzyme Activity ◽

Glutamate Dehydrogenase ◽

Bacillus Megaterium ◽

Glutamate Synthase ◽

Complete Loss ◽

Borate Buffer ◽

Arginine Residue ◽

Complete Protection ◽

Complete Inactivation ◽

Arginine Residues

Reaction of phenylglyoxal with glutamate dehydrogenase (EC 1.4.1.4), but not with glutamate synthase (EC 2.6.1.53), from Bacillus megaterium resulted in complete loss of enzyme activity. NADPH alone or together with 2-oxoglutarate provided substantial protection from inactivation by phenylglyoxal. Some 2mol of [14C]Phenylglyoxal was incorporated/mol of subunit of glutamate dehydrogenase. Addition of 1mM-NADPH decreased incorporation by 0.7mol. The Ki for phenylglyoxal was 6.7mM and Ks for competition with NADPH was 0.5mM. Complete inactivation of glutamate dehydrogenase by butane-2,3-dione was estimated by extrapolation to result from the loss of 3 of the 19 arginine residues/subunit. NADPH, but not NADH, provided almost complete protection against inactivation. Butane-2,3-dione had only a slight inactivating effect on glutamate synthase. The data suggest that an essential arginine residue may be involved in the binding of NADPH to glutamate dehydrogenase. The enzymes were inactivated by pyridoxal 5′-phosphate and this inactivation increased 3–4-fold in the borate buffer. NADPH completely prevented inactivation by pyridoxal 5′-phosphate.

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