IntEnz

EC 4.1.1.85 - 3-dehydro-L-gulonate-6-phosphate decarboxylase

IntEnz Enzyme Nomenclature
EC 4.1.1.85

Names

Reaction

• 14353 [IUBMB]
  3-dehydro-L-gulonate 6-phosphate

  3-dehydro-L-gulonate 6-phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:58774

  Formula: C6H8O10P
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  =

  CO₂

  CO2

  Name origin: UniProt - CHECKED (C)

  CHEBI:16526

  Formula: CO2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  L-xylulose 5-phosphate

  L-xylulose 5-phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:57829

  Formula: C5H9O8P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Cofactor

• Mg²⁺

Comments:

Requires Mg2+. Along with EC 5.1.3.22, L-ribulose-5-phosphate 3-epimerase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.

Links to other databases

References

1. Yew, W.S. and Gerlt, J.A.
   Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons.
   J. Bacteriol. 184 : 302-306 (2002). [PMID: 11741871]
2. Wise, E., Yew, W.S., Babbitt, P.C., Gerlt, J.A. and Rayment, I.
   Homologous (β/α)₈-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase.
   Biochemistry 41 : 3861-3869 (2002). [PMID: 11900527]

[EC 4.1.1.85 created 2005]