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A homodimer model can resolve the conundrum as to how cytochrome P450 oxidoreductase and cytochrome b5 compete for the same binding site on cytochrome P450c17. (Review)
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Data suggest CYP17A1, with electron donor NADPH-P450 reductase, is inherently distributive enzyme but that some processivity is present; some 17alpha-hydroxy pregnenolone formed does not dissociate from CYP17A1 before conversion to dehydroepiandrosterone; CYB5A does not enhance reaction by decreasing k(off) of ligands of CYP17A1. (CYP17A1 = cytochrome P450, family 17, subfamily A, polypeptide 1; CYB5A = cytochrome b5)
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Data suggest that cytochrome b5 (CYB5) and cytochrome b5 reductase 3 (CYB5R3) can reduce human cytoglobin (CYGB) and zebrafish cytoglobins at rates up to 250-fold higher than those reported for the known physiological substrates, hemoglobin and myoglobin; the three proteins (CYB5+CYB5R3+CYGB) appear to constitute a metabolon involved in generation of nitric oxide.
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Thus, although Mn-b5 binds to CYP17A1, it is unable to enhance the lyase reaction, strongly suggesting that cyt b5 has a redox effector role in enhancement of the CYP17A1 mediated lyase reaction necessary for androgen synthesis.
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This study constructed a model of the membrane-bound full-length human P450 1A2-cyt b5 complex. The model was assembled from several parts using a multiscale modeling approach covering all-atom and coarse-grained molecular dynamics (MD).
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We conclude that cytochrome b5 can influence the electronic conductivity of cytochrome P450c17 via allosteric, protein-protein interactions.
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Variants in CYB5A and CYB5R3 should be considered in the evaluation of breast cancer risk in African American women.
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CYB5A is the first RA susceptibility gene involved in androgen synthesis. Our functional analysis of SNP rs1790834 indicates that it contributes to the sex bias observed in RA.
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both area and ratio of 3betaHSD and CYB5A double positive cells, which could represent the hybrid cells of zona fasciculate and zona reticularis, are correlated with adrenal development and could influence age-related serum androstenedione levels.
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Two acidic residues, Glu-48 and Glu-49, of cytochrome b5 are essential for stimulating the 17,20-lyase activity of CYP17A1.
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raises the possibility that inhibition of CYB5A-deregulated downstream pathways, such as those involving TRAF6, may favor autophagy-mediated cancer cell death in selected subgroups of patients
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CYB5A, which has a role in stearyl-CoA-desaturase activity, and RNF10, with an unknown role in weight regulating pathways, associated with adiposity and nominally increased the risk for T2D in American Indians.
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Cytochrome b5 seems to play the key role in the formation of lipid-radical cycles in membranes.
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Results define CYB5A as a novel prognostic factor for PDAC that exerts its tumor-suppressor function through autophagy induction and TRAF6 modulation.
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CYP17A1/b5 interaction is stronger when the hydroxylase substrate pregnenolone is present in the CYP17A1 active site than when the lyase substrate 17alpha-hydroxypregnenolone is in the active site.
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Identification of the first human CYB5A missense mutation as the cause of isolated 17,20 lyase deficiency in three individuals with 46,XY disorder of sex development.
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Human adrenal cells that express both 3beta-hydroxysteroid dehydrogenase type 2 (HSD3B2) and cytochrome b5 (CYB5A) contribute to adrenal androstenedione production
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Cygb has a nitric-oxide dioxygenase function and ascorbate and cytochrome b(5) have roles as reductants
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We demonstrated 17,20-lyase deficiency due to an aberrant CytB5.
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novel cSNPs associated with significantly altered protein expression and/or hydroxylamine reduction activities, but only minimally impact overall observed phenotypic variability
