mannitol-1-phosphate 5-dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.17 | ||||||||
CAS no. | 9028-24-4 | ||||||||
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 | ||||||||
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In enzymology, a mannitol-1-phosphate 5-dehydrogenase (EC 1.1.1.17) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are D-mannitol 1-phosphate and NAD+, whereas its 3 products are fructose 6-phosphate, NADH and H+.
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-mannitol-1-phosphate:NAD+ 2-oxidoreductase. Other names in common use include hexose reductase, mannitol 1-phosphate dehydrogenase, D-mannitol-1-phosphate dehydrogenase, and fructose 6-phosphate reductase. This enzyme participates in fructose and mannose metabolism.
Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.
In enzymology, a shikimate dehydrogenase (EC 1.1.1.25) is an enzyme that catalyzes the chemical reaction
In enzymology, a sorbitol-6-phosphate dehydrogenase (EC 1.1.1.140) is an enzyme that catalyzes the chemical reaction
In enzymology, an erythrose-4-phosphate dehydrogenase (EC 1.2.1.72) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-arabinitol 4-dehydrogenase (EC 1.1.1.11) is an enzyme that catalyzes the chemical reaction
In enzymology, a fructose 5-dehydrogenase (NADP+) (EC 1.1.1.124) is an enzyme that catalyzes the chemical reaction
In enzymology, a fructuronate reductase (EC 1.1.1.57) is an enzyme that catalyzes the chemical reaction
In enzymology, a hydroxypyruvate reductase (EC 1.1.1.81) is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) is an enzyme that catalyzes the chemical reaction
In enzymology, a mannitol 2-dehydrogenase (EC 1.1.1.67) is an enzyme that catalyzes the chemical reaction
In enzymology, a mannitol 2-dehydrogenase (NADP+) (EC 1.1.1.138) is an enzyme that catalyzes the chemical reaction
In enzymology, a sorbose 5-dehydrogenase (NADP+) (EC 1.1.1.123) is an enzyme that catalyzes the chemical reaction
Tagaturonate reductase (EC 1.1.1.58) is an enzyme that catalyzes the chemical reaction
In enzymology, a glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) is an enzyme that catalyzes the chemical reaction
In enzymology, an orotate reductase (NADH) (EC 1.3.1.14) is an enzyme that catalyzes the chemical reaction
CDP-4-dehydro-6-deoxyglucose reductase (EC 1.17.1.1) is an enzyme that catalyzes the chemical reaction
In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction
In enzymology, a NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a nitrite reductase [NAD(P)H] (EC 1.7.1.4) is an enzyme that catalyzes the chemical reaction
The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.