1.2.1.27: methylmalonate-semialdehyde dehydrogenase (CoA-acylating)
This is an abbreviated version!
For detailed information about methylmalonate-semialdehyde dehydrogenase (CoA-acylating), go to the full flat file.
Word Map on EC 1.2.1.27
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1.2.1.27
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lysosomotropic
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3-hydroxyisobutyrate
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coa-dependent
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mississippi
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propionyl-coa
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aldh6a1
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3-hydroxypropionic
- 1.2.1.27
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lysosomotropic
- 3-hydroxyisobutyrate
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coa-dependent
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mississippi
- propionyl-coa
- aldh6a1
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3-hydroxypropionic
Reaction
Synonyms
Aldh6a1, dddC, FG99_15390, KES23460, malonate-semialdehyde dehydrogenase, methylmalonate semialdehyde dehydrogenase, methylmalonate semialdehyde dehydrogenase protein, methylmalonate-semialdehyde dehydrogenase, methylmalonic acid semialdehyde dehydrogenase, MGG_01606, MMSADH, MMSDH, MoMSDH, MSDH, NAD-dependent malonate-semialdehyde dehydrogenase, OdoMMSDH, OsALDH6, PA3570, SSO1218
ECTree
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Subunits
Subunits on EC 1.2.1.27 - methylmalonate-semialdehyde dehydrogenase (CoA-acylating)
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dimer
homodimer
tetramer
additional information
dimer of dimers, monomer consists of three domains, the dinucleotide binding domain comprising the residues 3123 and 141251, the catalytic domain with residues 252270, and a small domain, with residues 124140 and 471486
tetramer
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the monomeric structure is made up of two primary domains. Each has a central extended beta-sheet surrounded by alpha-helices, with a cleft between them which holds the cofactor. The second primary domain extends from residues 249 to 444 and has a central beta-sheet of seven strands surrounded by alpha-helices. This second beta-sheet is extended by the three beta-strands of the neighbouring dimer extension (residues 119-136 and 444-494) to make a beta-sheet of ten strands in the dimer structure. The finger extension (residues 119-136 and 444-480) forms a three-stranded beta-sheet extension which pulls the dimer structure together, but is also used as a hook to pull in a neighbouring dimer and form the basis of the hexameric structure
tetramer
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the monomeric structure is made up of two primary domains. Each has a central extended beta-sheet surrounded by alpha-helices, with a cleft between them which holds the cofactor. The second primary domain extends from residues 249 to 444 and has a central beta-sheet of seven strands surrounded by alpha-helices. This second beta-sheet is extended by the three beta-strands of the neighbouring dimer extension (residues 119-136 and 444-494) to make a beta-sheet of ten strands in the dimer structure. The finger extension (residues 119-136 and 444-480) forms a three-stranded beta-sheet extension which pulls the dimer structure together, but is also used as a hook to pull in a neighbouring dimer and form the basis of the hexameric structure
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each subunit consists of three distinct domains: an NAD-binding domain, a catalytic domain, and an oligomerization domain. Identification of key residues important for substrate recognition and tetrahedral intermediate stabilization. Two basic residues (Arg103 and Arg279) and six hydrophobic residues (Phe150, Met153, Val154, Trp157, Met281, and Phe449) are important for tetrahedral intermediate binding. The backbone amide of Cys280 and the side chain amine of Asn149 function as the oxyanion hole during the enzymatic reaction
additional information
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each subunit consists of three distinct domains: an NAD-binding domain, a catalytic domain, and an oligomerization domain. Identification of key residues important for substrate recognition and tetrahedral intermediate stabilization. Two basic residues (Arg103 and Arg279) and six hydrophobic residues (Phe150, Met153, Val154, Trp157, Met281, and Phe449) are important for tetrahedral intermediate binding. The backbone amide of Cys280 and the side chain amine of Asn149 function as the oxyanion hole during the enzymatic reaction
additional information
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each subunit consists of three distinct domains: an NAD-binding domain, a catalytic domain, and an oligomerization domain. Identification of key residues important for substrate recognition and tetrahedral intermediate stabilization. Two basic residues (Arg103 and Arg279) and six hydrophobic residues (Phe150, Met153, Val154, Trp157, Met281, and Phe449) are important for tetrahedral intermediate binding. The backbone amide of Cys280 and the side chain amine of Asn149 function as the oxyanion hole during the enzymatic reaction
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