Mannuronate reductase

mannuronate reductase
Identifiers
EC no.1.1.1.131
CAS no.37250-62-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

D-mannonic acid
 
 
 
H+
 
H+
 
D-mannuronic acid
 

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)).

References

  1. ^ Enzyme 1.1.1.131 at KEGG Pathway Database.
  2. ^ Farmer JJ, Eagon RG (January 1969). "Aldohexuronic acid catabolism by a soil Aeromonas". Journal of Bacteriology. 97 (1): 97–106. doi:10.1128/jb.97.1.97-106.1969. PMC 249554. PMID 4388117.