EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.2.2 | expressed as a GST-fusion protein in Escherichia coli | Photobacterium profundum |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.2.2 | determined at 1.05 A, revealing a hotdog hydrolase fold arranged as a dimer of dimers. A second crystal structure at 1.40 A iss obtained from a crystal that is grown in the presence of Mg2+, which reveals the presence of a binding site for divalent cations at a crystal contact. The Mg2+-bound structure shows localized conformational changes, and its active site is unoccupied, suggesting a mechanism to open the active site for substrate entry or product release | Photobacterium profundum |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.2.2 | D17A | mutant shows no activity | Photobacterium profundum |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.2.2 | Photobacterium profundum | Q93CG9 | - |
- |
3.1.2.2 | Photobacterium profundum SS9 | Q93CG9 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.2.2 | using affinity chromatography | Photobacterium profundum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.2.2 | 3-hydroxybutyryl-CoA + H2O | - |
Photobacterium profundum | CoA + 3-hydroxybutyrate | - |
? | |
3.1.2.2 | arachidonoyl-CoA + H2O | - |
Photobacterium profundum | CoA + arachidonate | - |
? | |
3.1.2.2 | arachidonoyl-CoA + H2O | - |
Photobacterium profundum SS9 | CoA + arachidonate | - |
? | |
3.1.2.2 | benzoyl-CoA + H2O | - |
Photobacterium profundum | CoA + benzoate | - |
? | |
3.1.2.2 | benzoyl-CoA + H2O | - |
Photobacterium profundum SS9 | CoA + benzoate | - |
? | |
3.1.2.2 | eicosapentaenoyl-CoA + H2O | - |
Photobacterium profundum | CoA + eicosapentaenoate | - |
? | |
3.1.2.2 | eicosapentaenoyl-CoA + H2O | - |
Photobacterium profundum SS9 | CoA + eicosapentaenoate | - |
? | |
3.1.2.2 | additional information | enzyme assays reveal that Orf6 has a higher specific activity toward long-chain fatty acyl-CoA substrates (palmitoyl-CoA and eicosapentaenoyl-CoA) than toward short-chain or aromatic acyl-CoA substrates | Photobacterium profundum | ? | - |
? | |
3.1.2.2 | additional information | enzyme assays reveal that Orf6 has a higher specific activity toward long-chain fatty acyl-CoA substrates (palmitoyl-CoA and eicosapentaenoyl-CoA) than toward short-chain or aromatic acyl-CoA substrates | Photobacterium profundum SS9 | ? | - |
? | |
3.1.2.2 | palmitoyl-CoA + H2O | - |
Photobacterium profundum | CoA + palmitate | - |
? | |
3.1.2.2 | palmitoyl-CoA + H2O | - |
Photobacterium profundum SS9 | CoA + palmitate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.2.2 | dimer | crystal structure, dimer of dimer | Photobacterium profundum |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.2.2 | Orf6 thioesterase | - |
Photobacterium profundum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.2.2 | 25 | - |
assay at | Photobacterium profundum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.2.2 | 7.5 | - |
assay at | Photobacterium profundum |