Mannuronate reductase

In enzymology, mannuronate reductase (EC 1.1.1.131) is an enzyme that catalyzes the chemical reaction

D-mannonic acid

+ NAD⁺

 

 

 

H⁺

 

H⁺

 

D-mannuronic acid

+ NADH

 

mannuronate reductase
Identifiers
EC no.	1.1.1.131
CAS no.	37250-62-7
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 D-mannonic acid and oxidised nicotinamide adenine dinucleotide (NAD⁺). Its products are D-mannuronic acid (shown in open-chain form), reduced NADH, and a proton. The enzyme can also use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.^[1][2]

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 D-mannonate:NAD(P)+ 6-oxidoreductase. Other names in common use include mannonate dehydrogenase, mannonate (nicotinamide adenine dinucleotide, (phosphate))dehydrogenase, mannonate dehydrogenase, mannuronate reductase, mannonate dehydrogenase (NAD(P)+), D-mannonate:nicotinamide adenine dinucleotide (phosphate, and oxidoreductase (D-mannuronate-forming)).