Selective inactivation of rabbit muscle glycerophosphate dehydrogenase by diazotized 3-aminopyridine adenine dinucleotide

Anderson, Bruce M.; Kohler, Susan T.; Anderson, Christopher R.

doi:10.1016/0003-9861(78)90374-0

Cited by 11 publications

(1 citation statement)

References 11 publications

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“…The thiol group is essential for enzyme activity as evidenced by the deactivation of the enzyme by treatment with reagents such as A-ethylmaleimide (Anderson et al, 1970). The sulfhydryl group is located in the cofactor site as suggested by the selective modification by 3-aminopyridine adenine dinucleotide (Anderson et al, 1978). The cofactor site is fairly hydrophobic although the pyrophosphate linkage in the cofactor is important for specific binding (Kim & Anderson, 1969).…”

Section: Discussionmentioning

confidence: 99%

Nonreductive interaction of vanadate with an enzyme containing a thiol group in the active site: glycerol-3-phosphate dehydrogenase

Crans¹,

Simone²

1991

Biochemistry

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The inhibitory effects of vanadium(V) were determined on the oxidation of glycerol 3-phosphate (G3P) catalyzed by glycerol-3-phosphate dehydrogenase (G3PDH), an enzyme with a thiol group in the active site. G3PDH from rabbit muscle was inhibited by vanadate, and the active inhibiting species were found to be the vanadate dimer and/or tetramer. The dimer was a sufficiently weak inhibitor at pH 7.4 with respect to G3P; the tetramer could account for all the observed inhibition. The tetramer was a competitive inhibitor with respect to G3P with a Ki of 0.12 mM. Both the dimer and tetramer were noncompetitive inhibitors at pH 7.4 with respect to NAD with Ki's of 0.36 mM and 0.67 mM. G3PDH inhibited by vanadate was reactivated when EDTA complexed the vanadate. The reactivation occurred even after extended periods of incubation of G3PDH and vanadate, suggesting that the inhibition is reversible despite the thiol group in the active site. Analogous reactivation is also observed with glyceraldehyde-3-phosphate dehydrogenase (Gly3PDH). Gly3PDH is an enzyme that previously had been reported to undergo redox chemistry with vanadate. The work described in this paper suggests vanadate will not necessarily undergo redox chemistry with enzymes containing thiol groups exposed on the surface of the protein.

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Section: Discussionmentioning

confidence: 99%

Nonreductive interaction of vanadate with an enzyme containing a thiol group in the active site: glycerol-3-phosphate dehydrogenase

Crans¹,

Simone²

1991

Biochemistry

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3-Aminopyridine 1,N6-ethenoadenine dinucleotide phosphate: A fluorescent reagent for NADP-requiring enzymes

Anderson

1983

Analytical Biochemistry

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Inactivation of chicken liver d-3-phosphoglycerate dehydrogenase by N-alkylmaleimides

Anderson

Dubler

1980

Archives of Biochemistry and Biophysics

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Selective inactivation of rabbit muscle glycerophosphate dehydrogenase by diazotized 3-aminopyridine adenine dinucleotide

Cited by 11 publications

References 11 publications

Nonreductive interaction of vanadate with an enzyme containing a thiol group in the active site: glycerol-3-phosphate dehydrogenase

Nonreductive interaction of vanadate with an enzyme containing a thiol group in the active site: glycerol-3-phosphate dehydrogenase

3-Aminopyridine 1,N6-ethenoadenine dinucleotide phosphate: A fluorescent reagent for NADP-requiring enzymes

Inactivation of chicken liver d-3-phosphoglycerate dehydrogenase by N-alkylmaleimides

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