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malfunction
loss-of-function cyp86B1/ralph mutants display a novel suberin monomer composition. Complete knockout of CYP86B1 in ralph1 and ralph2 leads to an almost complete lack of C22 and C24 omega-hydroxyacids and alpha,omega-dicarboxylic fatty acids in the seed coat polyester and is accompanied by a strong increase in C22 and C24 unsubstituted, saturated fatty acids
malfunction
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mutations in CYP703A2 or CYP704B1 genes result in pollen with remarkably similar zebra phenotypes (impaired pollen walls that lack a normal exine layer and exhibit a characteristic striped surface). Double and triple mutant combinations do not result in the appearance of novel phenotypes or enhancement of single mutant phenotypes
malfunction
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several diseases are genetically linked to the expression of CYP4 gene polymorphic variants, which may link human susceptibility to diseases of lipid metabolism and the activation and resolution phases of inflammation
malfunction
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suppression or knockout of sxe1 significantly reduces mating success in males throughout the diurnal cycle
metabolism
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CYP4A functions in liver fatty acid metabolism
metabolism
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CYP4A functions in liver fatty acid metabolism. Increased expression of the CYP4A omega hydroxylase during steatohepatitis and their induction in animals fed a high fat diet suggest they may play a pivotal role in preventing lipotoxicity, and may be responsible for induction of oxidative stress and progression to steatohepatitis. Omega-hydroxylation of the CYP2C arachidonic acid metabolite epoxyeicosatrienonic acid to omega-hydroxylated eicosatrienoic acid can induce peroxisome proliferation in rodents
metabolism
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CYP4A11 is the least efficient CYP450 omega-hydroxylase in PUFA metabolism. PUFA hydroxylation by CYP4A11 is low and only slightly regiospecific
metabolism
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the metabolomic profile of wild-type and sxe1 mutant males reveals that sxe1 likely functions as a fatty acid omega-hydroxylase, suggesting that male courtship and mating success is mediated by small compounds generated by this enzyme
metabolism
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multiple alkane hydroxylase systems ensure the utilization of substrates of a broad chain length range
metabolism
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multiple alkane hydroxylase systems ensure the utilization of substrates of a broad chain length range
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physiological function
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CYP omega-hydroxylase inhibition exerts significant anti-apoptosis effects, at least in part, by activation of ERK1/2 in ischemia/reperfusion heart. Inhibition reduces the infarct size of heart, decreases DNA fragmentation, reduces TUNEL-positive cells, attenuates caspase-3 activation, and modulates genes associated with apoptosis in rats rendered ischemia followed by reperfusion
physiological function
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CYP703A2 and CYP704B1 together with the fatty acyl reductase MALE STERILITY2 are required to provide an indispensable subset of fatty acid-derived components within the sporopollenin biosynthesis framework
physiological function
CYP86B1 is involved in polyester monomer biosynthesis during the course of plant development, has a role in suberin biogenesis
physiological function
is a key enzyme for aliphatic root suberin biosynthesis. In contrast to wild-type, no CYP86A1 transcript in total RNA from horst-1 seedlings (carries the T-DNA insertion in the first exon of CYP86A1) and horst-2 seedlings (T-DNA insertion is located in the second exon). Complemented CYP86A1-transformed horst-1 plants reveal a quantitative and qualitative aliphatic suberin composition similar to the wild-type
physiological function
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simultaneous operation of receptor and mechanical stimulations may synergistically amplify transmembrane Ca2+ mobilization through the activation of the non-voltage-gated Ca2+ entry/depolarization channel TRPC6, thereby enhancing the vascular tone via phospholipase C/diacylglycerol and phospholipase A(2)/omega-hydroxylase/20-hydroxyeicosatetraenoic acid pathways
physiological function
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simultaneous operation of receptor and mechanical stimulations may synergistically amplify transmembrane Ca2+ mobilization through the activation of the non-voltage-gated Ca2+ entry/depolarization channel TRPC6, thereby enhancing the vascular tone via phospholipase C/diacylglycerol and phospholipase A(2)/omega-hydroxylase/20-hydroxyeicosatetraenoic acid pathways. Activation of the cytosolic phospholipase A(2)/omega-hydroxylase cascade and consequent production of 20-hydroxyeicosatetraenoic acid is essential for the mechanical enhancement of receptor-activated TRPC6 current/channel activity
physiological function
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SXE1 is necessary for efficient male mating. Male-specific transcriptional regulator DSX(M) and the clock genes are necessary for cycling of sxe1 mRNA during the diurnal cycle
physiological function
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the alkane hydroxylase system of Pseudomonas putida GPo1 allows it to use alkanes as the sole source of carbon and energy. The alkane hydroxylase system of Pseudomonas putida GPo1 comprises three protein components: AlkB, soluble NADH-rubredoxin reductase, and soluble electron transfer protein rubredoxin. AlkB transfers one oxygen atom from O2 to the alkane molecule, while the other oxygen is reduced to H2O using the electrons provided by NADH-rubredoxin reductase via rubredoxin
physiological function
Q08KD8; Q08KD7 and Q08KD6; Q08KD5, Q08KE2; Q08KE1 and Q08KE0; Q08KD9 Mycobacterium sp. TY-6 has two distinct gene clusters for multicomponent monooxygenases involved in alkane oxidation. Propane is oxidized to 1-propanol through terminal oxidation in Mycobacterium sp. TY-6
physiological function
Q08KD8; Q08KD7 and Q08KD6; Q08KD5, Q08KE2; Q08KE1 and Q08KE0; Q08KD9 propane is oxidized to 1-propanol and 2-propanol through both terminal and subterminal oxidations in Pseudonocardia sp. TY-7
physiological function
Q08KD8; Q08KD7 and Q08KD6; Q08KD5, Q08KE2; Q08KE1 and Q08KE0; Q08KD9 Pseudonocardia sp. TY-7 has two distinct gene clusters for multicomponent monooxygenases involved in alkane oxidation. Propane is oxidized to 1-propanol through terminal oxidation in Mycobacterium sp. TY-6
physiological function
an AlkW1 gene knockout strain is able to grow with C28 n-alkane as the sole carbon source, presence of two further long-chain alkane hydroxylase genes G1 and G2 whose expression in induced upon growth on C28 n-alkane
physiological function
an isoform AlkB1 mutant demonstrates a markedly lower degradative rate for C21 to C32 n-alkanes compared to wild-type. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
physiological function
degradation of n-alkanes in Rhodococcus opacus R7 with consumption rates of 88% for n-dodecane, 69% for n-hexadecane, 51% for n-eicosane and 78% for n-tetracosane. Expression of the AlkB gene in Rhodococcus erythropolis leads to increased biodegradation of n-dodecane
physiological function
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for the medium-chain n-alkanes (C12-C16), single-knockout mutants of isoforms AlkB1 and AlkB2 show an obvious delay as compared to the wild type SJTD-1, and double-knockout mutants cannot utilize the n-alkanes at all. The loss of AlkB2 show a more pronounced effect on the cell growth than the loss of AlkB1. The poor viability of the double mutant recovers to a normal state when C18-C24 alkanes are used as the sole source of carbon
physiological function
isoform AlkB2 acts in the early growth phase and plays a major role in the utilization of C12-C18. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
physiological function
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one rubredoxin AlkG with two Fe-4S electron transfer centres can bind with two membrane-bound AlkB to form an AlkG:2AlkB adduct, facilitating an efficient conversion of n-octane to 1-octanol. the specific activity among all chain length linear alkanes tested varies, there is no particular relationship between the specific activity and the chain length of alkanes
physiological function
the expression of isoforms MAH1-1 and MAH1-2 is barely detected in stem and leaf of a wax deficient cultivar
physiological function
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degradation of n-alkanes in Rhodococcus opacus R7 with consumption rates of 88% for n-dodecane, 69% for n-hexadecane, 51% for n-eicosane and 78% for n-tetracosane. Expression of the AlkB gene in Rhodococcus erythropolis leads to increased biodegradation of n-dodecane
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physiological function
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the alkane hydroxylase system of Pseudomonas putida GPo1 allows it to use alkanes as the sole source of carbon and energy. The alkane hydroxylase system of Pseudomonas putida GPo1 comprises three protein components: AlkB, soluble NADH-rubredoxin reductase, and soluble electron transfer protein rubredoxin. AlkB transfers one oxygen atom from O2 to the alkane molecule, while the other oxygen is reduced to H2O using the electrons provided by NADH-rubredoxin reductase via rubredoxin
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physiological function
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isoform AlkB2 acts in the early growth phase and plays a major role in the utilization of C12-C18. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
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physiological function
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an isoform AlkB1 mutant demonstrates a markedly lower degradative rate for C21 to C32 n-alkanes compared to wild-type. An isoform AlkB1/AlkB2 a double mutant shows a trend towards recovery when C20-C24 are used as sole carbon source
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physiological function
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one rubredoxin AlkG with two Fe-4S electron transfer centres can bind with two membrane-bound AlkB to form an AlkG:2AlkB adduct, facilitating an efficient conversion of n-octane to 1-octanol. the specific activity among all chain length linear alkanes tested varies, there is no particular relationship between the specific activity and the chain length of alkanes
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physiological function
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for the medium-chain n-alkanes (C12-C16), single-knockout mutants of isoforms AlkB1 and AlkB2 show an obvious delay as compared to the wild type SJTD-1, and double-knockout mutants cannot utilize the n-alkanes at all. The loss of AlkB2 show a more pronounced effect on the cell growth than the loss of AlkB1. The poor viability of the double mutant recovers to a normal state when C18-C24 alkanes are used as the sole source of carbon
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additional information
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AlkB contains a nonheme diiron center as a catalytic site
additional information
both AlkW1 and AlkW2 have an integral-membrane alkane monooxygenase, AlkB, conserved domain and a rubredoxin conserved domain which are fused together
additional information
both AlkW1 and AlkW2 have an integral-membrane alkane monooxygenase, AlkB, conserved domain and a rubredoxin conserved domain which are fused together
additional information
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reconstitution of enzyme activity with the purified protein in an assay with purified rubredoxin, purified maize ferredoxin reductase, NADPH, and selected substrates. i.e. bicyclo[4.1.0]heptane (norcarane), bicyclo[3.1.0]hexane (bicyclohexane), methylphenylcyclopropane and deuterated and non-deuterated cyclohexane. Purified AbAlkB hydroxylates substrates by forming a substrate radical, the rate-determining step has a significant C-H bond breaking character
additional information
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the alkane hydroxylase system consists of the alkane hydroxylase large subunit, the alkane hydroxylase small subunit, the NADH-dependent reductase subunit, and the ferredoxin subunit. Analysis of the interaction between large and small subunits of the monooxygenase, overview
additional information
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AlkB contains a nonheme diiron center as a catalytic site
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