EC Number   |
General Information |
Reference |
|---|
    2.3.1.31 | evolution |
the organization of the catalytic domains' fold marks MetX as members of the alpha/beta-hydrolase superfamily. It is a highly diverse family that includes proteases, lipases, and esterases, among many others. A canonical 8-stranded beta-sheet fold with twisted, parallel topology forms the core of alpha/beta-hydrolases. Several alpha-helices flank either face of this fold, though their number and location are different depending on the specific protein. The catalytic domain comprises residues 15-181, 297-372 of MhMetX, residues 17-183, 304-379 of MaMetX, and residues 17-181, 311-372 of MtMetX. The catalytic domain contains the active site tunnel with its a canonical catalytic triad. The catalytic triad of nucleophile-His-acid is the alpha/beta-hydrolase family's most conserved feature. Just as in other known HTA structures, MtHTA, MhHTA, and MaHTA contain a serine, aspartic acid, and histidine in the active site. HTAs have a serine between beta7 and alpha3, an aspartic acid on the loop between beta9 and alpha6, and histidine on alpha7 for these residues. For MtHTA and MhHTA, Ser157, Asp320, and His350 comprise the active site. MaHTA's triad is comprised of Ser160, Asp327, His357. The catalytic serine sits at the end of a deep catalytic tunnel |
-, 758449 |
| 2.3.1.31 | malfunction |
enzyme enables the survival of fungi and bacteria in methionine-poor environments such as blood serum, thus its inhibition can be deleterious for the organism |
701784 |
| 2.3.1.31 | malfunction |
site-directed mutagenesis reveals that Bacillus cereus metA and Escherichia coli homoserine transsuccinylase share a common catalytic mechanism, glutamic acid 111 in the active site determines acetyl-CoA versus succinyl-CoA (glycine 111) specificity |
687796 |
| 2.3.1.31 | metabolism |
first step in the biosynthesis of methionine from aspartic acid |
701784 |
| 2.3.1.31 | metabolism |
methionine biosynthesis |
687796 |
| 2.3.1.31 | metabolism |
the enzyme reaction represents a critical control point for cell growth and viability |
735393 |
| 2.3.1.31 | metabolism |
the mycobacterial homoserine transacetylases is central to methionine biosynthesis |
-, 758449 |
| 2.3.1.31 | more |
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(15-70), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview |
758449 |
| 2.3.1.31 | more |
structure determination and comparison to structures of the Mycolicibacterium abscessus (MaMetX) and Mycolicibacterium tuberculosis (MtMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(77-372), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview |
-, 758449 |
| 2.3.1.31 | more |
structure determination and comparison to structures of the Mycolicibacterium tuberculosis (MtMetX) and Mycolicibacterium hassiacum (MhMetX) MetX enzymes, homology structure modelling with bound cofactors of MetX(10-379), analysis of the potential ligandability of MetX. Two copies of each monomer exist in the asymmetric unit of all three structures. MetX can be divided into two distinct structural domains, the catalytic domain, and the lid domain. Active site structure and catalytic mechanism, overview |
-, 758449 |
