Cytochrome P-450: Classification and Mechanism

This presentation explores the classification and mechanism of cytochrome P-450, a protein involved in enzymatic responses. Learn about the different subfamilies of enzymes, their structures, catalytic cycles, and spectroscopy. Discover the importance of cytochrome P-450 in biology and its impact on the human body.

CYTOCHROME P-450

INTRODUCTION
• The term cytochrome P-450 is defined as a
protein of the super family involving hame.
• Mainly, it uses numbers of minor and enormous
particles involve in the field of enzymatic
responses(Minerdi, et al., 2015).
• The aim of this presentation is to evaluate the
classification of cytochrome P-450 and their
mechanism.

CLASSIFICATION OF CYTOCHROME P-450
SUBFAMILY OF ENZYMES
• There are major five kinds of
cytochrome P-450 subfamily
such as:
• B-class (IPR002397)
• Mitochondrial (IPR002399)
• E-class, group I (IPR002401)
• E-class, group II (IPR002402)
(Hocum, et al., 2016).
(Source: Hocum, et al., 2016).

CLASSIFICATION OF CYTOCHROME P-450
SUBFAMILY OF ENZYMES
• Class B
• Class B enzymes were found to be freely proteins which
mainly communicate with NADH-specific FAD-containing.
• These enzymes are bacterial, mitochondrial or
fungalCYP55.
• Cytochrome P450, mitochondrial (IPR002399)
• In this process, cytochrome P450 can be decreased by
the 2Fe-2S iron-sulphur protein adrenodoxin
• Adrenodoxin and adrenodoxin reductase are soluble, and
all these are included in the field of mitochondrial
(IPR002399).

CLASSIFICATION OF CYTOCHROME P-450
SUBFAMILY OF ENZYMES
• Cytochrome P450, E-class, group I (IPR002401)
• There are major two components involve in E-class such
as NADPH:P450 reductase and P450.
• The class E enzymes are divided into five clusters where
each of them may involve more than single cytochrome
P450.
• Cytochrome P450, E-class, group II (IPR002402)
• Group II enzymes are mainly distributed widely in daily
life for example bacteria (Ahern, et al., 2017).
• Such kind of enzymes impact on the human body system
and increase the rate of bacteria.

MECHANISMS OF REGULATION OF
CYTOCHROME P-450
• The mechanisms of
regulation of cytochrome
is divided into major
three steps such as:
• Structure
• Catalytic cycle
• Spectroscopy
• All these steps provide a
platform for performing
cytochrome P-450. (Source: Liu, Rao, Li, & Li, 2015).

STRUCTURE
• It is observed that the lively place of cytochrome
includes numbers of heme-iron in the body.
• The firm is transmitted to the protein with the
help of cysteine ligand.
• Such kind of cysteine and few contiguous
deposits are preserved in un-defined CYPs
• Due to the numerous kinds of reactions catalyzed
by CYPs, and features of the different kinds of
CYPs differ in many aspects (Liu, Rao, Li, & Li,
2015).

CATALYTIC CYCLE
• There are following steps involve in the P450
catalytic cycle:
• Substrate obligatory produces a alteration in the
conformation of the energetic spot
• Sub section binding produce electron process developed
from NAD(P)H by using cytochrome P450 (Rasool, &
Mohamed, 2016).
• Molecular oxygen drags to the subsequent ferrous heme
which are centred at the distal axial
• The peroxo group delivered in stage 4 which is quickly
produced twice in the system and it also discharge one
particle of aquatic and framing the very receptive
classes.

SPECTROSCOPY
• Mainly, substrate is reproduced in the ghostly
possessions of the protein, with a growth in
absorbance at 390 nanometres
• Inhibitors parts which bind to the heme firm
increase the rate of type II spectrum
• It is analysed that the stability of process can be
maintained by reducing equivalents used in the
system (Capoferri, et al., 2015).

CONCLUSION
• It is concluded that the iron in Cytochrome P450
is tethered to the protein with the help of cysteine
thiolate ligand.
• This presentation classified different types of
Cytochrome P450 and also described the
fundamental mechanism of Cytochrome P450
• It is identified that there are major two classes of
Cytochrome P450 used in biologies such as class
B and class E.

REFERENCES
• Minerdi, D., Sadeghi, S. J., Di Nardo, G., Rua, F., Castrignanò, S., Allegra, P., & Gilardi, G. (2015).
CYP116B5: a new class VII catalytically self‐sufficient cytochrome P 450 from A cinetobacter
radioresistens that enables growth on alkanes. Molecular microbiology, 95(3), 539-554.
• Hocum, B. T., White Jr, J. R., Heck, J. W., Thirumaran, R. K., Moyer, N., Newman, R., & Ashcraft,
K. (2016). Cytochrome P-450 gene and drug interaction analysis in patients referred for
pharmacogenetic testing. American Journal of Health-System Pharmacy, 73(2), 61-67.
• Ahern, T. P., Hertz, D. L., Damkier, P., Ejlertsen, B., Hamilton-Dutoit, S. J., Rae, J. M., ... & Cronin-
Fenton, D. P. (2017). Cytochrome P-450 2D6 (CYP2D6) genotype and breast cancer recurrence
in tamoxifen-treated patients: evaluating the importance of loss of heterozygosity. American
journal of epidemiology, 185(2), 75-85.
• Liu, S., Rao, X. J., Li, M. Y., & Li, S. G. (2015). Identification and expression profiles of putative
cytochrome P 450 monooxygenase genes from C naphalocrocis medinalis (L epidoptera: P
yralidae). Entomological research, 45(3), 141-149.
• Rasool, S., & Mohamed, R. (2016). Plant cytochrome P450s: nomenclature and involvement in
natural product biosynthesis. Protoplasma, 253(5), 1197-1209.
• Capoferri, L., Verkade-Vreeker, M. C., Buitenhuis, D., Commandeur, J. N., Pastor, M., Vermeulen,
N. P., & Geerke, D. P. (2015). Linear interaction energy based prediction of cytochrome P450
1A2 binding affinities with reliability estimation. PLoS One, 10(11), e0142232.