Glucuronate reductase

In enzymology, a glucuronate reductase (EC 1.1.1.19) is an enzyme that catalyzes the chemical reaction

L-gulonic acid

+ NADP⁺

 

 

 

H⁺

 

H⁺

 

D-glucoronic acid

+ NADPH

 

L-glucuronate reductase
Identifiers
EC no.	1.1.1.19
CAS no.	9028-29-9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

The two substrates of this enzyme are L-gulonatic acid and oxidised nicotinamide adenine dinucleotide phosphate (NADP⁺). Its products are D-glucuronic acid, reduced NADPH, and a proton.^[1][2][3][4]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is L-gulonate:NADP⁺ 6-oxidoreductase. Other names in common use include aldehyde reductase, L-hexonate:NADP dehydrogenase, TPN-L-gulonate dehydrogenase, aldehyde reductase II, NADP-L-gulonate dehydrogenase, D-glucuronate dehydrogenase, D-glucuronate reductase, and L-glucuronate reductase (incorrect). This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.