putrescine oxidase | |||||||||
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Identifiers | |||||||||
EC no. | 1.4.3.10 | ||||||||
CAS no. | 9076-87-3 | ||||||||
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 putrescine oxidase (EC 1.4.3.10) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are putrescine, O2, and H2O, whereas its 3 products are 4-aminobutanal, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is putrescine:oxygen oxidoreductase (deaminating). This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, FAD.
Pyridoxine 5′-phosphate oxidase is an enzyme, encoded by the PNPO gene, that catalyzes several reactions in the vitamin B6 metabolism pathway. Pyridoxine 5′-phosphate oxidase catalyzes the final, rate-limiting step in vitamin B6 metabolism, the biosynthesis of pyridoxal 5′-phosphate, the biologically active form of vitamin B6 which acts as an essential cofactor. Pyridoxine 5′-phosphate oxidase is a member of the enzyme class oxidases, or more specifically, oxidoreductases. These enzymes catalyze a simultaneous oxidation-reduction reaction. The substrate oxidase enzymes is hydroxylated by one oxygen atom of molecular oxygen. Concurrently, the other oxygen atom is reduced to water. Even though molecular oxygen is the electron acceptor in these enzymes' reactions, they are unique because oxygen does not appear in the oxidized product.
In enzymology, a thiamine oxidase (EC 1.1.3.23) 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
Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:
In enzymology, a cyclohexylamine oxidase (EC 1.4.3.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-aspartate oxidase (EC 1.4.3.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-glutamate(D-aspartate) oxidase (EC 1.4.3.15) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-glutamate oxidase (EC 1.4.3.7) is an enzyme that catalyzes the chemical reaction
In enzymology, an ethanolamine oxidase (EC 1.4.3.8) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-lysine 6-oxidase (EC 1.4.3.20) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-lysine oxidase (EC 1.4.3.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a methanethiol oxidase (EC 1.8.3.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a nitroalkane oxidase (EC 1.7.3.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-methyl-L-amino-acid oxidase (EC 1.5.3.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a (S)-6-hydroxynicotine oxidase (EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction
Glycine oxidase (EC 1.4.3.19) is an enzyme with systematic name glycine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction
Polyamine oxidase (propane-1,3-diamine-forming) (EC 1.5.3.14, MPAO, maize PAO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming). This enzyme catalyses the following chemical reaction
Non-specific polyamine oxidase (EC 1.5.3.17, polyamine oxidase, Fms1, AtPAO3) is an enzyme with systematic name polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming). This enzyme catalyses the following chemical reaction