Cloned (Comment) | Organism |
---|---|
gene CD36-03230, recombinant expression in Escherichia coli | Candida dubliniensis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the enzyme shows positive cooperativity and substrate inhibition with some substrates. With benzaldehyde activity is observed, but the kinetic data cannot be fitted to Michaelis-Menten, cooperative or substrate inhibition kinetic models | Candida dubliniensis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
210000 | - |
crosslinking and gel filtration | Candida dubliniensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candida dubliniensis | B9W7C4 | - |
- |
Candida dubliniensis CD36 | B9W7C4 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxybenzaldehyde + NAD+ + H2O | - |
Candida dubliniensis | 4-hydroxybenzoate + NADH + 2 H+ | - |
? | |
4-hydroxybenzaldehyde + NAD+ + H2O | - |
Candida dubliniensis CD36 | 4-hydroxybenzoate + NADH + 2 H+ | - |
? | |
benzaldehyde + NAD+ + H2O | - |
Candida dubliniensis | benzoate + NADH + 2 H+ | - |
? | |
benzaldehyde + NAD+ + H2O | - |
Candida dubliniensis CD36 | benzoate + NADH + 2 H+ | - |
? | |
cyclohexanecarboxyaldehyde + NAD+ + H2O | - |
Candida dubliniensis | benzoate + NADH + 2 H+ | - |
? | |
cyclohexanecarboxyaldehyde + NAD+ + H2O | - |
Candida dubliniensis CD36 | benzoate + NADH + 2 H+ | - |
? | |
additional information | the enzyme has no detectable activity with vanillin suggesting that the annotation is incorrect. Molecular modeling of CD36-03230p demonstrates that it has an isoleucine residue (Ile156) at key position in the active site, instead of e.g. Met, further strengthening this hypothesis | Candida dubliniensis | ? | - |
? | |
additional information | the enzyme has no detectable activity with vanillin suggesting that the annotation is incorrect. Molecular modeling of CD36-03230p demonstrates that it has an isoleucine residue (Ile156) at key position in the active site, instead of e.g. Met, further strengthening this hypothesis | Candida dubliniensis CD36 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | crosslinking and gel filtration | Candida dubliniensis |
Synonyms | Comment | Organism |
---|---|---|
CD36-03230 | - |
Candida dubliniensis |
Cd36-03230p | - |
Candida dubliniensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Candida dubliniensis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the redox cofactor NADP+ and substrates increase the thermal stability of the protein, thermal stabilities (Tm) of Cd36_03230p in the presence of various potential substrates, overview | Candida dubliniensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
assay at | Candida dubliniensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | structure-based multiple sequence alignment shows conserved residues at both NAD(P)+ binding and catalytic domains | Candida dubliniensis | |
NAD+ | - |
Candida dubliniensis | |
NADP+ | - |
Candida dubliniensis |
General Information | Comment | Organism |
---|---|---|
additional information | enzyme molecular modeling, dimeric model construction using the structure of ALDH domains of Geobacter sulfurreducens PutA, PDB ID 4NMB, for the enzyme dimer and sheep liver class 1 aldehyde dehydrogenase structure, 1BXS, as the template fo rthe tetramer. molecularmodelling of Cd36_03230p predicts that it has a similar fold to other aldehyde dehydrogenases | Candida dubliniensis |