Monooxygenases are enzymes that incorporate one
hydroxyl group (−OH) into substrates in many metabolic pathways. In this reaction, the two atoms of
dioxygen
There are several known allotropes of oxygen. The most familiar is molecular oxygen (O2), present at significant levels in Earth's atmosphere and also known as dioxygen or triplet oxygen. Another is the highly reactive ozone (O3). Others are:
* ...
are reduced to one
hydroxyl group and one H
2O molecule by the concomitant oxidation of
NAD(P)H
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 aden ...
.
One important subset of the monooxygenases, the
cytochrome P450 omega hydroxylase Cytochrome P450 omega hydroxylases, also termed cytochrome P450 ω-hydroxylases, CYP450 omega hydroxylases, CYP450 ω-hydroxylases, CYP omega hydroxylase, CYP ω-hydroxylases, fatty acid omega hydroxylases, cytochrome P450 monooxygenases, and fatty ...
s, is used by cells to metabolize arachidonic acid (i.e. eicosatetraenoic acid) to the
cell signaling
In biology, cell signaling (cell signalling in British English) or cell communication is the ability of a cell to receive, process, and transmit signals with its environment and with itself. Cell signaling is a fundamental property of all cellula ...
molecules,
20-hydroxyeicosatetraenoic acid or to reduce or totally inactivate the activate signaling molecules for example by hydroxylating
leukotriene B4
Leukotriene B4 (LTB4) is a leukotriene involved in inflammation. It has been shown to promote insulin resistance in obese mice.
Biochemistry
Leukotriene B4 (LTB4) is a leukotriene involved in inflammation. It is produced from leukocytes in r ...
to 20-hydroxy-leukotriene B5,
5-hydroxyeicosatetraenoic acid to 5,20-dihydroxyeicosatetraenoic acid,
5-oxo-eicosatetraenoic acid to 5-oxo-20-hydroxyeicosatetraenoic acid,
12-hydroxyeicosatetraenoic acid to 12,20-dihydroxyeicosatetraenoic acid, and
epoxyeicosatrienoic acids to 20-hydroxy-epoxyeicosatrienoic acids.
Classification
They are classified as
oxidoreductase
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually u ...
enzymes that catalyzes an electron transfer.
Related structures
2XDO2XYO2Y6R
Human proteins containing this domain
COQ6
Coenzyme Q6 monooxygenase is a protein that in humans is encoded by the COQ6 gene.
Function
The protein encoded by this gene belongs to the ubiH/COQ6 family. It is an evolutionarily conserved monooxygenase required for the biosynthesis of coenz ...
;
CYP450
Cytochromes P450 (CYPs) are a superfamily of enzymes containing heme as a cofactor that functions as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compo ...
;
MICAL1
NEDD9-interacting protein with calponin homology and LIM domains is a protein that in humans is encoded by the ''MICAL1'' gene.
Interactions
MICAL1 has been shown to interact with NEDD9 and RAB1A
Ras-related protein Rab-1A is a protein that in ...
;
MICAL2
Protein MICAL-2 is a protein that in humans is encoded by the ''MICAL2'' gene
In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth' ...
;
MICAL2PV1;
MICAL2PV2;
MICAL3
Microtubule-associated monoxygenase, calponin and LIM domain containing 3, also known as MICAL3, is a human gene.
Function
Along with two other Rab proteins, Rab6 and Rab8, MICAL3 work together in the process of docking and fusing of vesicles t ...
;
See also
*
ABM domain
In molecular biology, the ABM domain is a protein domain that is found in monooxygenases involved in the biosynthesis of several antibiotics by ''Streptomyces'' species, which can carry out oxygenation without the assistance of any of the prosth ...
References
External links
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{{Oxygenases
Protein domains
Enzymes