5-exo-hydroxycamphor dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.327 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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5-exo-hydroxycamphor dehydrogenase (EC 1.1.1.327, F-dehydrogenase, FdeH) is an enzyme with systematic name 5-exo-hydroxycamphor:NAD+ oxidoreductase. [1] [2] [3] This enzyme catalyses the following chemical reaction
This enzyme contains Zn2+. It is isolated from Pseudomonas putida .
Glutamate dehydrogenase is an enzyme observed in both prokaryotes and eukaryotic mitochondria. The aforementioned reaction also yields ammonia, which in eukaryotes is canonically processed as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has a very low affinity for ammonia, and therefore toxic levels of ammonia would have to be present in the body for the reverse reaction to proceed. However, in brain, the NAD+/NADH ratio in brain mitochondria encourages oxidative deamination. In bacteria, the ammonia is assimilated to amino acids via glutamate and aminotransferases. In plants, the enzyme can work in either direction depending on environment and stress. Transgenic plants expressing microbial GLDHs are improved in tolerance to herbicide, water deficit, and pathogen infections. They are more nutritionally valuable.
Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene.
In enzymology, an ephedrine dehydrogenase (EC 1.5.1.18) is an enzyme that catalyzes the chemical reaction
In enzymology, a carnitine 3-dehydrogenase (EC 1.1.1.108) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC 1.1.1.178) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxyisobutyrate dehydrogenase also known as β-hydroxyisobutyrate dehydrogenase or 3-hydroxyisobutyrate dehydrogenase, mitochondrial (HIBADH) is an enzyme that in humans is encoded by the HIBADH gene.
In enzymology, a cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase (EC 1.3.1.29) is an enzyme that catalyzes the chemical reaction
In enzymology, a cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase (EC 1.3.1.67) is an enzyme that catalyzes the chemical reaction
In enzymology, a cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.56) is an enzyme that catalyzes the chemical reaction
In enzymology, a cis-dihydroethylcatechol dehydrogenase (EC 1.3.1.66) is an enzyme that catalyzes the chemical reaction
In enzymology, a camphor 5-monooxygenase (EC 1.14.15.1) is an enzyme that catalyzes the chemical reaction
In enzymology, an aminobutyraldehyde dehydrogenase (EC 1.2.1.19) is an enzyme that catalyzes the chemical reaction
In enzymology, a gamma-guanidinobutyraldehyde dehydrogenase (EC 1.2.1.54) is an enzyme that catalyzes the chemical reaction
Inosine-5′-monophosphate dehydrogenase (IMPDH) is a purine biosynthetic enzyme that catalyzes the nicotinamide adenine dinucleotide (NAD+)-dependent oxidation of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), the first committed and rate-limiting step towards the de novo biosynthesis of guanine nucleotides from IMP. IMPDH is a regulator of the intracellular guanine nucleotide pool, and is therefore important for DNA and RNA synthesis, signal transduction, energy transfer, glycoprotein synthesis, as well as other process that are involved in cellular proliferation.
Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. This enzyme catalyses the following chemical reaction
2-Hydroxymuconate-6-semialdehyde dehydrogenase (EC 1.2.1.85, xylG [gene], praB [gene] ) is an enzyme with systematic name (2E,4Z)-2-hydroxy-6-oxohexa-2,4-dienoate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD+). Members of the NADH dehydrogenase family and analogues are commonly systematically named using the format NADH:acceptor oxidoreductase. The chemical reaction these enzymes catalyze is generally represented with the following equation:
2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108, 2,5-diketocamphane lactonizing enzyme, ketolactonase I, 2,5-diketocamphane 1,2-monooxygenase oxygenating component, 2,5-DKCMO, camphor 1,2-monooxygenase, camphor ketolactonase I) is an enzyme with systematic name (+)-bornane-2,5-dione,NADH:oxygen oxidoreductase (1,2-lactonizing). This enzyme catalyses the following chemical reaction
6-hydroxy-3-succinoylpyridine 3-monooxygenase (EC 1.14.13.163, 6-hydroxy-3-succinoylpyridine hydroxylase, hspA (gene), hspB (gene)) is an enzyme with systematic name 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate,NADH:oxygen oxidoreductase (3-hydroxylating, succinate semialdehyde releasing). This enzyme catalyses the following chemical reaction
Putidaredoxin—NAD+ reductase (EC 1.18.1.5, putidaredoxin reductase, camA (gene)) is an enzyme with systematic name putidaredoxin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction