Localization of Cytochrome P450 in Membranes: Mitochondria

Omura, Tsuneo

doi:10.1007/978-3-642-77763-9_4

Cited by 12 publications

(6 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1). This observation strongly supports the inference that mitochondrial P450s evolved from microsomal P450s (Omura, 1993). Among them CYP4L6 could be of ancient origin and CYP333B1 and -333B2 could be a very recent expansion of CYP333B subfamily based on their gene structure and sequence identity.…”

Section: Genomic Distribution Of P450 Superfamily In the Silkwormsupporting

confidence: 79%

Genome-wide analysis of cytochrome P450 monooxygenase genes in the silkworm, Bombyx mori

Zhu

Duan

et al. 2011

Gene

View full text Add to dashboard Cite

Section: Genomic Distribution Of P450 Superfamily In the Silkwormsupporting

confidence: 79%

Genome-wide analysis of cytochrome P450 monooxygenase genes in the silkworm, Bombyx mori

Zhu

Duan

et al. 2011

Gene

View full text Add to dashboard Cite

“…The cytochrome P450 enzyme class is widely distributed in various forms of life and participates in diversified metabolic reactions as the oxygen-activating component of monooxygenase systems (1,2). Its unique oxygenation chemistry and its substrate specificity offer the opportunity to develop enzymatic systems for synthesizing fine chemicals, sensing biochemically active compounds, and detoxifying environmental contamination.…”

mentioning

confidence: 99%

“…As shown in Fig. 1 (Upper), the overall biocatalytic cycle is composed of many individual reactions (1,2,6). The two electrons necessary for the reaction are supplied by reduced putidaredoxin Pdx r , a 2Fe-2S protein (11.6 kDa), which mediates the transfer of these electrons from NADH and the FAD-containing putidaredoxin reductase PdR to the heme active center of the cytochrome CYP101 (45 kDa).…”

mentioning

confidence: 99%

A direct electrode-driven P450 cycle for biocatalysis

Reipa

Mayhew²,

Vilker³

1997

Proc. Natl. Acad. Sci. U.S.A.

106

View full text Add to dashboard Cite

The large potential of redox enzymes to carry out formation of high value organic compounds motivates the search for innovative strategies to regenerate the cofactors needed by their biocatalytic cycles. Here, we describe a bioreactor where the reducing power to the cycle is supplied directly to purified cytochrome CYP101 (P450cam; EC 1.14.15.1) through its natural redox partner (putidaredoxin) using an antimony-doped tin oxide working electrode. Required oxygen was produced at a Pt counter electrode by water electrolysis. A continuous catalytic cycle was sustained for more than 5 h and 2,600 enzyme turnovers. The maximum product formation rate was 36 nmol of 5-exo-hydroxycamphor͞nmol of CYP101 per min.

show abstract

“…CYP4C7 contains a region of high sequence similarity to other members of the CYP4 family ( Fig. 1), and several CYP4 enzymes of vertebrates have been implicated in -hydroxylation of fatty acids as well as leukotriene hydroxylation (30). CYP4C1 of another cockroach, Blaberus discoidalis, is a P450 expressed in the fat body that is thought to be involved in lipid mobilization under the control of the hypertrehalosemic hormone (35).…”

Section: Discussionmentioning

confidence: 99%

A cytochrome P450 terpenoid hydroxylase linked to the suppression of insect juvenile hormone synthesis

Sutherland

Unnithan

Andersen

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

121

View full text Add to dashboard Cite

A cDNA encoding a cytochrome P450 enzyme was isolated from a cDNA library of the corpora allata (CA) from reproductively active Diploptera punctata cockroaches. This P450 from the endocrine glands that produce the insect juvenile hormone (JH) is most closely related to P450 proteins of family 4 and was named CYP4C7. The CYP4C7 gene is expressed selectively in the CA; its message could not be detected in the fat body, corpora cardiaca, or brain, but trace levels of expression were found in the midgut and caeca. The levels of CYP4C7 mRNA in the CA, measured by ribonuclease protection assays, were linked to the activity cycle of the glands. In adult females, CYP4C7 expression increased immediately after the peak of JH synthesis, reaching a maximum on day 7, just before oviposition. mRNA levels then declined after oviposition and during pregnancy. The CYP4C7 protein was produced in Escherichia coli as a C-terminal His-tagged recombinant protein. In a reconstituted system with insect NADPH cytochrome P450 reductase, cytochrome b 5 , and NADPH, the purified CYP4C7 metabolized (2E,6E)-farnesol to a more polar product that was identified by GC-MS and by NMR as (10E)-12-hydroxyfarnesol. CYP4C7 converted JH III to 12-trans-hydroxy JH III and metabolized other JH-like sesquiterpenoids as well. This -hydroxylation of sesquiterpenoids appears to be a metabolic pathway in the corpora allata that may play a role in the suppression of JH biosynthesis at the end of the gonotrophic cycle.Juvenile hormone (JH) plays a central role in insect development, metamorphosis, and reproduction. This sesquiterpenoid epoxide is synthesized in endocrine glands, the corpora allata (CA)(1), and is degraded predominantly by esterases and epoxide hydrolases (2). The rate of JH synthesis by the CA is a major determinant of the titer of JH in the hemolymph (3), and the regulation of JH synthesis is seen as a potential target for insect control. The biosynthesis of JH has been extensively characterized during the reproductive cycle of the cockroach Diploptera punctata, an insect that serves as a convenient model system. In adult females of this insect, the cycle of JH synthesis is regulated by humoral factors and by innervation from neurosecretory cells in the brain (1). Production of JH by the CA increases 10-fold to reach a peak 5 days after adult emergence and mating, and this peak corresponds to the peak of vitellogenesis. Synthesis is then rapidly repressed and remains low from deposition of the eggs into the brood sac through pregnancy (4).The allatostatins, a family of brain-gut peptides (5-9) are known to inhibit JH synthesis in D. punctata at the end of a gonotrophic cycle, but these peptides are probably not alone responsible for repression of the intrinsic rate of JH synthesis in postvitellogenic insects. The mechanism of stable suppression of JH synthesis at the end of the cycle has received very little attention, in part because of the absence of molecular tools to dissect it. This repression occurs concomitant with changes in c...

show abstract

Localization of Cytochrome P450 in Membranes: Mitochondria

Cited by 12 publications

References 30 publications

Genome-wide analysis of cytochrome P450 monooxygenase genes in the silkworm, Bombyx mori

Genome-wide analysis of cytochrome P450 monooxygenase genes in the silkworm, Bombyx mori

A direct electrode-driven P450 cycle for biocatalysis

A cytochrome P450 terpenoid hydroxylase linked to the suppression of insect juvenile hormone synthesis

Contact Info

Product

Resources

About