Cloned (Comment) | Organism |
---|---|
gene dddC, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Oceanimonas doudoroffii |
Crystallization (Comment) | Organism |
---|---|
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-methyl-3-oxopropanoate + CoA + H2O + NAD+ | Oceanimonas doudoroffii | - |
propanoyl-CoA + HCO3- + NADH | - |
? | |
2-methyl-3-oxopropanoate + CoA + H2O + NAD+ | Oceanimonas doudoroffii ATCC 27123 | - |
propanoyl-CoA + HCO3- + NADH | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oceanimonas doudoroffii | G5CZI2 | - |
- |
Oceanimonas doudoroffii ATCC 27123 | G5CZI2 | - |
- |
Purification (Comment) | Organism |
---|---|
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-methyl-3-oxopropanoate + CoA + H2O + NAD+ | - |
Oceanimonas doudoroffii | propanoyl-CoA + HCO3- + NADH | - |
? | |
2-methyl-3-oxopropanoate + CoA + H2O + NAD+ | - |
Oceanimonas doudoroffii ATCC 27123 | propanoyl-CoA + HCO3- + NADH | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 54000, SDS-PAGE, in solution | Oceanimonas doudoroffii |
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 | Comment | Organism |
---|---|---|
dddC | - |
Oceanimonas doudoroffii |
methylmalonate-semialdehyde dehydrogenase | - |
Oceanimonas doudoroffii |
MMSDH | - |
Oceanimonas doudoroffii |
OdoMMSDH | - |
Oceanimonas doudoroffii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Oceanimonas doudoroffii |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the aldehyde dehydrogenase superfamily | Oceanimonas doudoroffii |
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 |
physiological function | the enzyme is involved in the decarboxylation of methylmalonate-semialdehyde (MMSA) downstream of the dimethylsulfoniopropionate (DMSP) cleavage pathway | Oceanimonas doudoroffii |