Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.1.67 extracted from

  • Datta, S.; Annapure, U.; Timson, D.
    Characterization of Cd36-03230p, a putative vanillin dehydrogenase from Candida dubliniensis (2016), RSC Adv., 6, 99774-99780 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene CD36-03230, recombinant expression in Escherichia coli Candida dubliniensis

KM Value [mM]

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 [Da] Molecular Weight Maximum [Da] Comment Organism
210000
-
crosslinking and gel filtration Candida dubliniensis

Organism

Organism UniProt Comment Textmining
Candida dubliniensis B9W7C4
-
-
Candida dubliniensis CD36 B9W7C4
-
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
tetramer crosslinking and gel filtration Candida dubliniensis

Synonyms

Synonyms Comment Organism
CD36-03230
-
Candida dubliniensis
Cd36-03230p
-
Candida dubliniensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Candida dubliniensis

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
assay at Candida dubliniensis

Cofactor

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

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