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UDP-glucuronic acid dehydrogenase

Class of enzymes

Class of enzymes

FieldValue
NameUDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)
EC_number1.1.1.305

UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) (, UDP-GlcUA decarboxylase, ArnADH) is an enzyme with systematic name UDP-glucuronate:NAD+ oxidoreductase (decarboxylating). This enzyme catalyses the following chemical reaction

: UDP-glucuronate + NAD+ \rightleftharpoons UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+

The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13 (UDP-4-amino-4-deoxy-L-arabinose formyltransferase).

References

References

  1. (April 2005). "A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose". The Journal of Biological Chemistry.
  2. (October 2004). "Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance". Biochemistry.
  3. (June 2005). "Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis". The Journal of Biological Chemistry.
  4. (June 2005). "Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance". Structure.
  5. (December 2007). "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli". The Journal of Biological Chemistry.
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ec-1.1.1
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