|Background:||Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine salvage pathway that catalyzes the continuous reactions of 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone metabolite using Mg2+ as cofactor. In this study, we have determined the crystal structure of MASA and its complex with a substrate analog to 1.7A resolution by multi-wavelength anomalous diffraction and molecular replacement techniques, respectively.|
|Structure Weight:||29316.11 Da|
|Chain Length:||285 amino acids|
|Ligand Chemical Component:||Selenomethionine|
|Reference:||Wang, H., Pang, H., Bartlam, M., Rao, Z. (2005) Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase J.Mol.Biol. 348: 917-926|
|Synonyms:||DKFZp586M0524; E1; FLJ12594; MASA; MST145; E-1 enzyme; Enolase-phosphatase E1; MSTP145 protein; acireductone synthase; EC 220.127.116.11; 2,3-diketo-5-methylthio-1-phosphopentane phosphatase; MASA homolog|
|Function:||magnesium ion binding; phosphor-glycolate phosphatase activity; acireductone synthase activity; metal ion binding; catalytic activity|
Price does not include shipping and packaging costs.Request quote for final price.