Application | Comment | Organism |
---|---|---|
synthesis | the engineered enzyme mutant H144L/W187F is used for production of 4-hydroxyvaleric acid, a monomer of bio-polyester and a precursor of bio-fuels, from levulinic acid | Alcaligenes faecalis |
Cloned (Comment) | Organism |
---|---|
expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) | Alcaligenes faecalis |
Protein Variants | Comment | Organism |
---|---|---|
H144L/W187F | site-directed mutagenesis, the mutant shows activity with levulinnic acid, in contrast to the wild-type enzyme, and is engineered for production of 4-hydroxyvaleric acid, molecular docking simulation, overview | Alcaligenes faecalis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-3-hydroxybutanoate + NAD+ | Alcaligenes faecalis | - |
acetoacetate + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alcaligenes faecalis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography | Alcaligenes faecalis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-3-hydroxybutanoate + NAD+ | - |
Alcaligenes faecalis | acetoacetate + NADH + H+ | - |
r | |
additional information | no activity of the wild-type enzyme with levulinic acid, enzyme mutant H144L/W187F is active with levulinic acid producing 4-hydroxyvaleric acid | Alcaligenes faecalis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3HBDH | - |
Alcaligenes faecalis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
reduction reaction | Alcaligenes faecalis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
reduction reaction | Alcaligenes faecalis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Alcaligenes faecalis |
General Information | Comment | Organism |
---|---|---|
additional information | Gln94, His144, Lys152, and Gln196 form hydrogen bonds with carboxyl and/or ketone group of acetoacetate, Trp187, Trp257 form hydrophobic interactions with the carbon atoms of acetoacetate, and Ser142 and Tyr155 are directly related to the catalytic mechanism | Alcaligenes faecalis |