2.3.1.31: homoserine O-acetyltransferase
This is an abbreviated version!
For detailed information about homoserine O-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.31
-
2.3.1.31
-
l-methionine
-
ping-pong
-
o-acetylhomoserine
-
acetyl-enzyme
-
succinyl-coa
-
sulfhydrylase
-
gamma-hydroxyl
-
o-acetyl-l-homoserine
-
medicine
-
molecular biology
-
drug development
- 2.3.1.31
- l-methionine
-
ping-pong
- o-acetylhomoserine
-
acetyl-enzyme
- succinyl-coa
-
sulfhydrylase
-
gamma-hydroxyl
- o-acetyl-l-homoserine
- medicine
- molecular biology
- drug development
Reaction
Synonyms
acetyltransferase, homoserine, CnHTA, DcsE, HAT, homoserine acetyltransferase, homoserine O-acetyltransferase, homoserine transacetylase, homoserine transsuccinylase, homoserine-O-transacetylase, HTA, HTS, L-homoserine O-acetyltransferase, MaHTA, MaMetX, MET2, MetA, MetX, MetXA, metX_1, metX_2, MhHTA, MhMetX, MsHAT, MtHTA, MtMetX, TmHTS
ECTree
Advanced search results
General Information
General Information on EC 2.3.1.31 - homoserine O-acetyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
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
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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
-
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
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
-
first step in the biosynthesis of methionine from aspartic acid
metabolism
-
the enzyme reaction represents a critical control point for cell growth and viability
metabolism
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
metabolism
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
metabolism
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
metabolism
-
the mycobacterial homoserine transacetylases is central to methionine biosynthesis
-
enzyme MsHAT catalyzes the transfer of acetyl-group from acetyl-CoA to homoserine
physiological function
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
physiological function
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
physiological function
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
the homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of the methionine biosynthesis pathway
-
physiological function
-
enzyme MsHAT catalyzes the transfer of acetyl-group from acetyl-CoA to homoserine
-
the enzyme displays a high sequence homology to L-homoserine O-acetyltransferase, but it prefers L-serine over L-homoserine as the substrate, structure analysis and modeling, overview
additional information
-
the enzyme structure belongs to the alpha/beta-hydrolase superfamily, consisting of two distinct domains: a core alpha/beta-domain containing the catalytic site and a lid domain assembled into a helical bundle. The active site consists of a classical catalytic triad located at the end of a deep tunnel, structure comparisons, overview. The reaction catalyzed by the enzyme involves the acetylation of the gamma-hydroxyl of homoserine through an acetyl-CoA-dependent acetylation via a double-displacement mechanism facilitated by a classic Ser-His-Asp catalytic triad which is located at the bottom of a narrow tunnel
additional information
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
additional information
-
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
additional information
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
additional information
-
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
additional information
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
additional information
substrate binding mode and molecular mechanism of MsHAT, detailed overview. Enzyme structure comparisons. The active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HAT enzymes. The conserved Ser152, His345, and Asp315 residues form a catalytic triad, and they act as a covalent nucleophile, a general base, and an electron donor, respectively. Arg222, Asp346, Tyr229, and Tyr260 residues are mainly involved in the binding of homoserine or acetyl-CoA and other residues are not crucial for the stabilization of its substrates
additional information
-
substrate binding mode and molecular mechanism of MsHAT, detailed overview. Enzyme structure comparisons. The active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HAT enzymes. The conserved Ser152, His345, and Asp315 residues form a catalytic triad, and they act as a covalent nucleophile, a general base, and an electron donor, respectively. Arg222, Asp346, Tyr229, and Tyr260 residues are mainly involved in the binding of homoserine or acetyl-CoA and other residues are not crucial for the stabilization of its substrates
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
the enzyme displays a high sequence homology to L-homoserine O-acetyltransferase, but it prefers L-serine over L-homoserine as the substrate, structure analysis and modeling, overview
-
additional information
-
substrate binding mode and molecular mechanism of MsHAT, detailed overview. Enzyme structure comparisons. The active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HAT enzymes. The conserved Ser152, His345, and Asp315 residues form a catalytic triad, and they act as a covalent nucleophile, a general base, and an electron donor, respectively. Arg222, Asp346, Tyr229, and Tyr260 residues are mainly involved in the binding of homoserine or acetyl-CoA and other residues are not crucial for the stabilization of its substrates
-