cd01629

Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep

CDD entry
Member databaseCDD
CDD typedomain
Short nameHAD_EP
SetHAD_like

Description

Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
[4, 3, 2, 1]

References

1.Appendix. Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca. Balakrishnan R, Frohlich M, Rahaim PT, Backman K, Yocum RR. J. Biol. Chem. 268, 24792-5, (1993). View articlePMID: 8227040

2.Mutagenesis of the enolase-phosphatase gene in Xanthomonas oryzae pv. oryzae affects growth on methylthioadenosine and in vivo S-adenosylmethionine pools. Zhang Y, Zhang G, Zhang J, Wang X, Wang J. Arch Microbiol 191, 773-83, (2009). PMID: 19730818

3.Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes. Burroughs AM, Allen KN, Dunaway-Mariano D, Aravind L. J. Mol. Biol. 361, 1003-34, (2006). View articlePMID: 16889794

4.Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity. Wang H, Pang H, Bartlam M, Rao Z. J. Mol. Biol. 348, 917-26, (2005). View articlePMID: 15843022

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