aryl-aldehyde oxidase | |||||||||
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Identifiers | |||||||||
EC no. | 1.2.3.9 | ||||||||
CAS no. | 82657-93-0 | ||||||||
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, an aryl-aldehyde oxidase (EC 1.2.3.9) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are aromatic aldehyde, O2, and H2O, whereas its two products are aromatic carboxylic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is aryl-aldehyde:oxygen oxidoreductase.
Xanthine oxidase is a form of xanthine oxidoreductase, a type of enzyme that generates reactive oxygen species. These enzymes catalyze the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. These enzymes play an important role in the catabolism of purines in some species, including humans.
A peroxy acid is an acid which contains an acidic –OOH group. The two main classes are those derived from conventional mineral acids, especially sulfuric acid, and the peroxy derivatives of organic carboxylic acids. They are generally strong oxidizers.
In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction
In enzymology, an aryl-alcohol oxidase (EC 1.1.3.7) is an enzyme that catalyzes the chemical reaction
Long-chain alcohol oxidase is one of two enzyme classes that oxidize long-chain or fatty alcohols to aldehydes. It has been found in certain Candida yeast, where it participates in omega oxidation of fatty acids to produce acyl-CoA for energy or industrial use, as well as in other fungi, plants, and bacteria.
In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction
In enzymology, an abscisic-aldehyde oxidase (EC 1.2.3.14) is an enzyme that catalyzes the chemical reaction
In enzymology, an aryl-aldehyde dehydrogenase (NADP+) (EC 1.2.1.30) is an enzyme that catalyzes the chemical reaction
In enzymology, a glyoxylate oxidase (EC 1.2.3.5) is an enzyme that catalyzes the chemical reaction
In enzymology, an indole-3-acetaldehyde oxidase (EC 1.2.3.7) is an enzyme that catalyzes the chemical reaction
In enzymology, an oxalate oxidase (EC 1.2.3.4) is an oxalate degrading enzyme that catalyzes the chemical reaction:
In enzymology, a retinal oxidase (EC 1.2.3.11) 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, a L-glutamate oxidase (EC 1.4.3.11) 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
The Pinnick oxidation is an organic reaction by which aldehydes can be oxidized into their corresponding carboxylic acids using sodium chlorite (NaClO2) under mild acidic conditions. It was originally developed by Lindgren and Nilsson. The typical reaction conditions used today were developed by G. A. Kraus. H.W. Pinnick later demonstrated that these conditions could be applied to oxidize α,β-unsaturated aldehydes. There exist many different reactions to oxidize aldehydes, but only a few are amenable to a broad range of functional groups. The Pinnick oxidation has proven to be both tolerant of sensitive functionalities and capable of reacting with sterically hindered groups. This reaction is especially useful for oxidizing α,β-unsaturated aldehydes, and another one of its advantages is its relatively low cost.
Ent-kaurenoic acid oxidase (EC 1.14.13.79) is an enzyme with systematic name ent-kaur-16-en-19-oate,NADPH:oxygen oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction