Cat. No.

CBCRY26

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.

Molecular description

Protein Classification

Hydrolase

Structure Weight

29316.11 Da

Polymer

1

Molecule

E-1 Enzyme

Chain Length

285 amino acids

Crystal Description

PDB ID

1ZS9

MMDB ID

33918

Source

E.coli

Method

X-Ray Diffraction

Resolution

1.7Å

Ligand Chemical Component

Selenomethionine

Gene information

Gene Name

ENOPH1

Synonyms

DKFZp586M0524; E1; FLJ12594; MASA; MST145; E-1 enzyme; Enolase-phosphatase E1; MSTP145 protein; acireductone synthase;  EC 3.1.3.77; 2,3-diketo-5-methylthio-1-phosphopentane phosphatase; MASA homolog

UniProt ID

Q9UHY7

GeneID

58478

Chromosome  Location

4q21.22

Function

magnesium ion binding; phosphor-glycolate phosphatase activity; acireductone synthase activity; metal ion binding; catalytic activity

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