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Literature summary extracted from

  • Do, H.; Lee, C.W.; Lee, S.G.; Kang, H.; Park, C.M.; Kim, H.J.; Park, H.; Park, H.; Lee, J.H.
    Crystal structure and modeling of the tetrahedral intermediate state of methylmalonate-semialdehyde dehydrogenase (MMSDH) from Oceanimonas doudoroffii (2016), J. Microbiol., 54, 114-121 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.27 gene dddC, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Oceanimonas doudoroffii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.27 purified recombinant His6-tagged enzyme, mixing of 0.001 ml of protein solution containing 32.2 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 1 mM DTT, with 0.001 ml of reservoir solution consisting of 21% PEG 3350 and 0.2 M potassium sodium tartrate, pH 7.5, at 20°C, 2 days, X-ray diffraction sructure determination and analysis at 2.9 A resolution, Among the twelve molecules in the asymmetric unit, six subunits complexed with NAD+ Oceanimonas doudoroffii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.27 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ Oceanimonas doudoroffii
-
 propanoyl-CoA + HCO3- + NADH
-
 ?
1.2.1.27 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ Oceanimonas doudoroffii ATCC 27123
-
 propanoyl-CoA + HCO3- + NADH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.27 Oceanimonas doudoroffii G5CZI2
-
-
1.2.1.27 Oceanimonas doudoroffii ATCC 27123 G5CZI2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.27 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3). Among the twelve molecules in the asymmetric unit, six subunits complexed with NAD+ Oceanimonas doudoroffii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.27 2-methyl-3-oxopropanoate + CoA + H2O + NAD+
-
 Oceanimonas doudoroffii propanoyl-CoA + HCO3- + NADH
-
 ?
1.2.1.27 2-methyl-3-oxopropanoate + CoA + H2O + NAD+
-
 Oceanimonas doudoroffii ATCC 27123 propanoyl-CoA + HCO3- + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.27 homodimer 2 * 54000, SDS-PAGE, in solution Oceanimonas doudoroffii
1.2.1.27 More 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 Oceanimonas doudoroffii

Synonyms

EC Number Synonyms Comment Organism
1.2.1.27 dddC
-
 Oceanimonas doudoroffii
1.2.1.27 methylmalonate-semialdehyde dehydrogenase
-
 Oceanimonas doudoroffii
1.2.1.27 MMSDH
-
 Oceanimonas doudoroffii
1.2.1.27 OdoMMSDH
-
 Oceanimonas doudoroffii

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.27 NAD+
-
 Oceanimonas doudoroffii

General Information

EC Number General Information Comment Organism
1.2.1.27 evolution the enzyme is a member of the aldehyde dehydrogenase superfamily Oceanimonas doudoroffii
1.2.1.27 additional information 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 Oceanimonas doudoroffii
1.2.1.27 physiological function the enzyme is involved in the decarboxylation of methylmalonate-semialdehyde (MMSA) downstream of the dimethylsulfoniopropionate (DMSP) cleavage pathway Oceanimonas doudoroffii