ExplorEnz: EC 1.1.1.428

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1.1.1.428

Accepted name:

4-methylthio 2-oxobutanoate reductase (NADH)

Reaction:

(2R)-2-hydroxy-4-(methylsulfanyl)butanoate + NAD⁺ = 4-(methylsulfanyl)-2-oxobutanoate + NADH + H⁺

Other name(s):

CTBP1 (gene name); C-terminal-binding protein 1; MTOB reductase; 4-methylthio 2-oxobutyrate reductase; 4-methylthio 2-oxobutyric acid reductase

Systematic name:

(2R)-2-hydroxy-4-(methylsulfanyl)butanoate:NAD⁺ 2-oxidoreductase

Comments:

The substrate of this enzyme is formed as an intermediate during L-methionine salvage from S-methyl-5′-thioadenosine, which is formed during the biosynthesis of polyamines. The human enzyme also functions as a transcriptional co-regulator that downregulates the expression of many tumor-suppressor genes, thus providing a link between gene repression and the methionine salvage pathway. A similar, but NADP-specific, enzyme is involved in dimethylsulfoniopropanoate biosynthesis in algae and phytoplankton.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Kumar, V., Carlson, J.E., Ohgi, K.A., Edwards, T.A., Rose, D.W., Escalante, C.R., Rosenfeld, M.G. and Aggarwal, A.K. Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase. Mol. Cell 10 (2002) 857–869. [DOI] [PMID: 12419229]
2.	Achouri, Y., Noel, G. and Van Schaftingen, E. 2-Keto-4-methylthiobutyrate, an intermediate in the methionine salvage pathway, is a good substrate for CtBP1. Biochem. Biophys. Res. Commun. 352 (2007) 903–906. [DOI] [PMID: 17157814]
3.	Hilbert, B.J., Grossman, S.R., Schiffer, C.A. and Royer, W.E., Jr. Crystal structures of human CtBP in complex with substrate MTOB reveal active site features useful for inhibitor design. FEBS Lett. 588 (2014) 1743–1748. [DOI] [PMID: 24657618]
4.	Korwar, S., Morris, B.L., Parikh, H.I., Coover, R.A., Doughty, T.W., Love, I.M., Hilbert, B.J., Royer, W.E., Jr., Kellogg, G.E., Grossman, S.R. and Ellis, K.C. Design, synthesis, and biological evaluation of substrate-competitive inhibitors of C-terminal Binding Protein (CtBP). Bioorg. Med. Chem. 24 (2016) 2707–2715. [DOI] [PMID: 27156192]

[EC 1.1.1.428 created 2022]