The oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is an enzyme complex, most commonly known for its role in the citric acid cycle.
Homogentisic acid is a phenolic acid usually found in Arbutus unedo (strawberry-tree) honey. It is also present in the bacterial plant pathogen Xanthomonas campestris pv. phaseoli as well as in the yeast Yarrowia lipolytica where it is associated with the production of brown pigments. It is oxidatively dimerised to form hipposudoric acid, one of the main constituents of the 'blood sweat' of hippopotamuses.
Enzyme catalysis is the increase in the rate of a process by a biological molecule, an "enzyme". Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site.
Pyruvate dehydrogenase kinase is a kinase enzyme which acts to inactivate the enzyme pyruvate dehydrogenase by phosphorylating it using ATP.
Amine Dehydrogenase, also known as methylamine dehydrogenase (MADH), is a tryptophan tryptophylquinone-dependent (TTQ-dependent) enzyme that catalyzes the oxidative deamination of a primary amine to an aldehyde and ammonia. The reaction occurs as follows:
Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene.
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial is an enzyme that in humans is encoded by the PDHA1 gene.The pyruvate dehydrogenase complex is a nuclear-encoded mitochondrial matrix multienzyme complex that provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle by catalyzing the irreversible conversion of pyruvate into acetyl-CoA. The PDH complex is composed of multiple copies of 3 enzymes: E1 (PDHA1); dihydrolipoyl transacetylase (DLAT) ; and dihydrolipoyl dehydrogenase (DLD). The E1 enzyme is a heterotetramer of 2 alpha and 2 beta subunits. The E1-alpha subunit contains the E1 active site and plays a key role in the function of the PDH complex.
Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 is an enzyme that in humans is encoded by the AKR1C1 gene.
Pyruvate dehydrogenase kinase isoform 2 (PDK2) also known as pyruvate dehydrogenase lipoamide kinase isozyme 2, mitochondrial is an enzyme that in humans is encoded by the PDK2 gene. PDK2 is an isozyme of pyruvate dehydrogenase kinase.
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.
Maximilian Nierenstein was a professor of biochemistry at the University of Bristol.
3-Dehydroshikimic acid is a chemical compound related to shikimic acid. 3-DHS is available in large quantity through engineering of the shikimic acid pathway.
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase (EC 1.1.1.335, WlbA, WbpB) is an enzyme with systematic name UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate:NAD+ 3-oxidoreductase. This enzyme catalyses the following chemical reaction:
Methanol dehydrogenase (cytochrome c) (EC 1.1.2.7, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction
Alcohol dehydrogenase (azurin) (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB) is an enzyme with systematic name alcohol:azurin oxidoreductase. This enzyme catalyses the following chemical reaction
Short-chain acyl-CoA dehydrogenase is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction
Primary-amine oxidase, also known as semicarbazide-sensitive amine oxidase (SSAO), is an enzyme (EC 1.4.3.21) with the systematic name primary-amine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction
Aralkylamine dehydrogenase (azurin) (EC 1.4.9.2, aromatic amine dehydrogenase, arylamine dehydrogenase, tyramine dehydrogenase) is an enzyme with the systematic name aralkylamine:azurin oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction:
Lupanine 17-hydroxylase (cytochrome c) (EC 1.17.2.2, lupanine dehydrogenase (cytochrome c)) is an enzyme with systematic name lupanine:cytochrome c-oxidoreductase (17-hydroxylating). This enzyme catalyses the following chemical reaction
Caffeine dehydrogenase, commonly referred to in scientific literature as caffeine oxidase, is an enzyme with the systematic name caffeine:ubiquinone oxidoreductase. The enzyme is most well known for its ability to directly oxidize caffeine, a type of methylxanthine, to trimethyluric acid. Caffeine dehydrogenase can be found in bacterium Pseudomonas sp. CBB1 and in several species within the genera Alcaligenes, Rhodococcus, and Klebsiella.
