From Wikipedia, the free encyclopedia
3-(hydroxyamino)phenol mutase
Identifiers
EC no. 5.4.4.3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a 3-(hydroxyamino)phenol mutase ( EC 5.4.4.3) is an enzyme that catalyzes the chemical reaction

3-hydroxyaminophenol aminohydroquinone

Hence, this enzyme has one substrate, 3-hydroxyaminophenol, and one product, aminohydroquinone.

This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. The systematic name of this enzyme class is 3-(hydroxyamino)phenol hydroxymutase. Other names in common use include 3-hydroxylaminophenol mutase, and 3HAP mutase.

References

  • Schenzle A, Lenke H, Spain JC, Knackmuss HJ (March 1999). "3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 catalyzes a Bamberger rearrangement". Journal of Bacteriology. 181 (5): 1444–50. PMC  93532. PMID  10049374.


From Wikipedia, the free encyclopedia
3-(hydroxyamino)phenol mutase
Identifiers
EC no. 5.4.4.3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a 3-(hydroxyamino)phenol mutase ( EC 5.4.4.3) is an enzyme that catalyzes the chemical reaction

3-hydroxyaminophenol aminohydroquinone

Hence, this enzyme has one substrate, 3-hydroxyaminophenol, and one product, aminohydroquinone.

This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. The systematic name of this enzyme class is 3-(hydroxyamino)phenol hydroxymutase. Other names in common use include 3-hydroxylaminophenol mutase, and 3HAP mutase.

References

  • Schenzle A, Lenke H, Spain JC, Knackmuss HJ (March 1999). "3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 catalyzes a Bamberger rearrangement". Journal of Bacteriology. 181 (5): 1444–50. PMC  93532. PMID  10049374.



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