Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-Hydroxybenzyl alcohol | mixed-type inhibition of 4-cresol oxidation | Geobacter metallireducens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0017 | - |
4-Cresol | - |
Geobacter metallireducens | |
0.0027 | - |
4-Hydroxybenzyl alcohol | - |
Geobacter metallireducens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | a tightly membrane-bound PCMH complex exists in anaerobic organisms in contrast to aerobic ones, where the enzyme is soluble and periplasmic, nevertheless the membrane complex has soluble components, overview | Geobacter metallireducens | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | cytochrome c-containing enzyme | Geobacter metallireducens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-cresol + 2 acceptor + H2O | Geobacter metallireducens | PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol | 4-hydroxybenzaldehyde + 2 reduced acceptor | - |
? | |
4-hydroxybenzyl alcohol + acceptor | Geobacter metallireducens | PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol | 4-hydroxybenzaldehyde + reduced acceptor | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacter metallireducens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
380fold purification of the soluble components including the active site of the enzyme membrane complex by membrane preparation, solubilization of the complex with lauryldimethylamine N-oxide, gel filtration, and hydrophobic interaction chromatography | Geobacter metallireducens |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
2.2 | - |
purified soluble components including the active site of the enzyme membrane complex | Geobacter metallireducens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-cresol + 2 acceptor + H2O | PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol | Geobacter metallireducens | 4-hydroxybenzaldehyde + 2 reduced acceptor | - |
? | |
4-cresol + Fe3+ + H2O | PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors | Geobacter metallireducens | 4-hydroxybenzaldehyde + Fe2+ | - |
? | |
4-hydroxybenzyl alcohol + acceptor | PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol | Geobacter metallireducens | 4-hydroxybenzaldehyde + reduced acceptor | - |
? | |
4-hydroxybenzyl alcohol + Fe3+ + H2O | PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors | Geobacter metallireducens | 4-hydroxybenzaldehyde + Fe2+ | - |
? | |
additional information | functional modelling, overview | Geobacter metallireducens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme complex shows a unique alphaalpha'beta2 subunit composition, with alpha and alpha' representing isoforms of the FAD-containing subunit and beta representing a c-type cytochrome | Geobacter metallireducens |
Synonyms | Comment | Organism |
---|---|---|
p-cresol methylhydroxylase | - |
Geobacter metallireducens |
PCMH | - |
Geobacter metallireducens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome | the enzyme complex shows a a unique alphaalpha'beta2 subunit composition, with beta representing a c-type cytochrome | Geobacter metallireducens | |
FAD | the enzyme complex shows a unique alphaalpha'beta2 subunit composition, with alpha and alpha' representing isoforms of the FAD-containing subunit, one FAD is covalently linked to Tyr394 of the alpha subunit. In contrast, the alpha' subunit does not contain any FAD cofactor and is therefore considered to be catalytically inactive | Geobacter metallireducens |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.018 | - |
4-Hydroxybenzyl alcohol | competitive inhibition | Geobacter metallireducens | |
0.235 | - |
4-Hydroxybenzyl alcohol | uncompetitive inhibition | Geobacter metallireducens |