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Chemical Compound Review:

AGN-PC-00IWN3 [5-(6-aminopurin-9-yl)-4- hydroxy-2...

Synonyms: AC1L18DJ

Ma, Y.C. et al., Komuniecki, R. et al., Dickinson, J.R. et al., Komuniecki, R. et al., Goetzman, E.S. et al., et al.

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High impact information on alpha-methylbutanoyl-CoA

Enzyme assay of the patient's fibroblasts, using 2-methylbutyryl-CoA as substrate, confirmed the defect [1].
However, recombinant St-IVD1 had maximal activity with 2-methylbutyryl-CoA, which in humans is dehydrogenated by short/branched-chain acyl-CoA dehydrogenase (SBCAD) [2].
The first, via branched chain alpha-ketoacid dehydrogenase to alpha-methylbutyryl-CoA, was eliminated because abolition of branched-chain alpha-ketoacid dehydrogenase in an lpd1 disruption mutant did not prevent the formation of active amyl alcohol [3].
Incubations of A. suum submitochondrial particles with NADH, 2-methylcrotonyl-CoA, purified A. suum electron-transfer flavoprotein and 2-methyl branched-chain enoyl-CoA reductase resulted in significant 2-methylbutyryl-CoA formation, which was inhibited by both rotenone and antisera to the purified ETF-RO [4].
Incubations of A. suum submitochondrial particles, NADH, tiglyl-CoA, purified A. suum electron-transfer flavoprotein, and the 2-methyl branched-chain acyl-CoA dehydrogenase resulted in the rotenone-sensitive, dehydrogenase-dependent formation of 2-methylbutyryl-CoA [5].

Biological context of alpha-methylbutanoyl-CoA

Dehydrogenase activity was greatest with 2-methylbutyryl CoA and the relative substrate specificities of the ascarid dehydrogenase(s) differ greatly from their mammalian counterparts [6].

Gene context of alpha-methylbutanoyl-CoA

No transferase activity was apparent from 2-methylbutyryl-CoA or 2-methylvaleryl-CoA as was previously reported for the nematode, Ascaris suum [7].

References

Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Andresen, B.S., Christensen, E., Corydon, T.J., Bross, P., Pilgaard, B., Wanders, R.J., Ruiter, J.P., Simonsen, H., Winter, V., Knudsen, I., Schroeder, L.D., Gregersen, N., Skovby, F. Am. J. Hum. Genet. (2000) [Pubmed]
Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum tuberosum. Goetzman, E.S., Mohsen, A.W., Prasad, K., Vockley, J. J. Biol. Chem. (2005) [Pubmed]
An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae. Dickinson, J.R., Harrison, S.J., Dickinson, J.A., Hewlins, M.J. J. Biol. Chem. (2000) [Pubmed]
Purification and characterization of electron-transfer flavoprotein: rhodoquinone oxidoreductase from anaerobic mitochondria of the adult parasitic nematode, Ascaris suum. Ma, Y.C., Funk, M., Dunham, W.R., Komuniecki, R. J. Biol. Chem. (1993) [Pubmed]
Purification and characterization of the 2-methyl branched-chain Acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum. Komuniecki, R., Fekete, S., Thissen-Parra, J. J. Biol. Chem. (1985) [Pubmed]
2-Methylbutyryl CoA dehydrogenase from mitochondria of Ascaris suum and its relationship to NADH-dependent 2-methylcrotonyl CoA reduction. Komuniecki, R., Fekete, S., Thissen, J. Biochem. Biophys. Res. Commun. (1984) [Pubmed]
Acyl-CoA transferase activities in homogenates of Fasciola hepatica adults. Saz, H.J., deBruyn, B., de Mata, Z. J. Parasitol. (1996) [Pubmed]

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