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Literature summary for 1.97.1.2 extracted from

  • Reichenbecher, W.; Schink, B.
    Towards the reaction mechanism of pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici (1999), Biochim. Biophys. Acta, 1430, 245-253.
    View publication on PubMed
Search for more literature for 1.97.1.2

Metals/Ions

Metals/Ions Comment Organism Structure
Fe
-
 Pelobacter acidigallici

Organism

Organism UniProt Comment Textmining
Pelobacter acidigallici
-
-
-

Oxidation Stability

Oxidation Stability Organism
oxides replace the physiological cosubstrate, p.e. pyridine N-oxide, 2-hydroxypyridine N-oxide, DMSO and tetramethylene sulfoxide Pelobacter acidigallici

Reaction

Reaction Comment Organism Reaction ID
1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene a mechanism is proposed which combines an oxidative hydroxylation with a reductive dehydroxylation via molybdenum cofactor Pelobacter acidigallici
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 oxides tested as cosubstrates Pelobacter acidigallici

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2,3,5-tetrahydroxybenzene + hydroxyhydroquinone
-
 Pelobacter acidigallici phloroglucinol + 1,2,4,5-tetrahydroxybenzene
-
 ?
1,2,3,5-tetrahydroxybenzene + pyrogallol pyrogallol i.e. 1,2,3-tri-hydroxybenzene Pelobacter acidigallici phloroglucinol + 1,2,3,5-tetrahydroxybenzene phloroglucinol i.e. 1,3,5-tri-hydroxybenzene ?
additional information pyrogallol converts to phloroglucinol in the absence of added tetrahydroxybenzene if very little pyrogallol and high amounts of enzyme are present Pelobacter acidigallici ?
-
 ?
additional information water is not the source of the added hydroxyl groups Pelobacter acidigallici ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
molybdenum cofactor
-
 Pelobacter acidigallici