Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | required | Alcanivorax borkumensis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
150000 | - |
above, native enzyme, gel filtration | Alcanivorax borkumensis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
octane + reduced rubredoxin + O2 | Alcanivorax borkumensis | - |
1-octanol + oxidized rubredoxin + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alcanivorax borkumensis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme is solubilized from membranes and further purified by anion exchange chromatography and gel filtration | Alcanivorax borkumensis |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:n-octane-grown cell | - |
Alcanivorax borkumensis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
bicyclohexane + reduced rubredoxin + O2 | i.e. bicyclo[3.1.0]hexane, no distinction between the 2- and 3-positions, reaction via formation of a substrate radical that persists in the active site | Alcanivorax borkumensis | ? + oxidized rubredoxin + H2O | - |
? | |
methylphenylcyclopropane + reduced rubredoxin + O2 | reaction via formation of a substrate radical that persists in the active site | Alcanivorax borkumensis | 1-phenylbut-3-en-1-ol + oxidized rubredoxin + H2O | - |
? | |
additional information | AbAlkB can catalyze the hydroxylation of a large number of aromatic compounds and linear and cyclic alkanes. It does not catalyze the hydroxylation of alkanes with a chain length longer than 15 carbons, nor does it hydroxylate sterically hindered C-H bonds. GC-MS product analysis, overview. AbAlkB hydroxylates the terminal methyl group of medium chain alkanes, where octane is apparently close to the optimal chain length | Alcanivorax borkumensis | ? | - |
? | |
norcarane + reduced rubredoxin + O2 | i.e. bicyclo[4.1.0]heptane, oxidation preferentially occurs at the less sterically hindered 3-position, reaction via formation of a substrate radical that persists in the active site | Alcanivorax borkumensis | ? + oxidized rubredoxin + H2O | - |
? | |
octane + reduced rubredoxin + O2 | - |
Alcanivorax borkumensis | 1-octanol + oxidized rubredoxin + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
alkane hydroxylase | - |
Alcanivorax borkumensis |
AlkB | - |
Alcanivorax borkumensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Alcanivorax borkumensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Alcanivorax borkumensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
rubredoxin | i.e. AlkG | Alcanivorax borkumensis |
General Information | Comment | Organism |
---|---|---|
additional information | reconstitution of enzyme activity with the purified protein in an assay with purified rubredoxin, purified maize ferredoxin reductase, NADPH, and selected substrates. i.e. bicyclo[4.1.0]heptane (norcarane), bicyclo[3.1.0]hexane (bicyclohexane), methylphenylcyclopropane and deuterated and non-deuterated cyclohexane. Purified AbAlkB hydroxylates substrates by forming a substrate radical, the rate-determining step has a significant C-H bond breaking character | Alcanivorax borkumensis |