PMID- 27875967
OWN - NLM
STAT- MEDLINE
DCOM- 20180101
LR  - 20190201
IS  - 1875-5550 (Electronic)
IS  - 1389-2037 (Linking)
VI  - 19
IP  - 1
DP  - 2018
TI  - Microbial P450 Enzymes in Bioremediation and Drug Discovery: Emerging Potentials 
      and Challenges.
PG  - 75-86
LID - 10.2174/1389203718666161122105750 [doi]
AB  - Cytochrome P450 enzymes are a structurally conserved but functionally diverse 
      group of heme-containing mixed function oxidases found across both prokaryotic 
      and eukaryotic forms of the microbial world. Microbial P450s are known to perform 
      diverse functions ranging from the synthesis of cell wall components to 
      xenobiotic/drug metabolism to biodegradation of environmental chemicals. 
      Conventionally, many microbial systems have been reported to mimic mammalian 
      P450-like activation of drugs and were proposed as the in-vitro models of 
      mammalian drug metabolism. Recent reports suggest that native or engineered forms 
      of specific microbial P450s from these and other microbial systems could be 
      employed for desired specific biotransformation reactions toward natural and 
      synthetic (drug) compounds underscoring their emerging potential in drug 
      improvement and discovery. On the other hand, microorganisms particularly fungi 
      and actinomycetes have been shown to possess catabolic P450s with unusual 
      potential to degrade toxic environmental chemicals including persistent organic 
      pollutants (POPs). Wood-rotting basidiomycete fungi in particular have revealed 
      the presence of exceptionally large P450 repertoire (P450ome) in their genomes, 
      majority of which are however orphan (with no known function). Our pre- and 
      post-genomic studies have led to functional characterization of several fungal 
      P450s inducible in response to exposure to several environmental toxicants and 
      demonstration of their potential in bioremediation of these chemicals. This 
      review is an attempt to summarize the postgenomic unveiling of this versatile 
      enzyme superfamily in microbial systems and investigation of their potential to 
      synthesize new drugs and degrade persistent pollutants, among other 
      biotechnological applications.
CI  - Copyright(c) Bentham Science Publishers; For any queries, please email at 
      epub@benthamscience.org.
FAU - Bhattacharya, Sukanta S
AU  - Bhattacharya SS
AD  - Microbial Pathogenesis and Toxicogenomics Laboratory, Department of Environmental 
      Health, College of Medicine, University of Cincinnati, Cincinnati, Ohio 
      45267-0056, OH, USA.
FAU - Yadav, Jagjit S
AU  - Yadav JS
AD  - Microbial Pathogenesis and Toxicogenomics Laboratory, Department of Environmental 
      Health, College of Medicine, University of Cincinnati, Cincinnati, Ohio 
      45267-0056, OH, USA.
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United Arab Emirates
TA  - Curr Protein Pept Sci
JT  - Current protein & peptide science
JID - 100960529
RN  - 9035-51-2 (Cytochrome P-450 Enzyme System)
SB  - IM
MH  - Animals
MH  - Bacteria/*enzymology
MH  - Biodegradation, Environmental
MH  - Biotechnology/*methods
MH  - Cytochrome P-450 Enzyme System/chemistry/genetics/*metabolism
MH  - Drug Discovery/*methods
MH  - Humans
MH  - Protein Engineering
OTO - NOTNLM
OT  - Cytochrome P450
OT  - bioremediation
OT  - drug discovery
OT  - drug metabolism
OT  - hydroxylation.
OT  - motifs
OT  - xenobiotics
EDAT- 2016/11/24 06:00
MHDA- 2018/01/02 06:00
CRDT- 2016/11/24 06:00
PHST- 2016/05/05 00:00 [received]
PHST- 2016/08/30 00:00 [revised]
PHST- 2016/10/04 00:00 [accepted]
PHST- 2016/11/24 06:00 [pubmed]
PHST- 2018/01/02 06:00 [medline]
PHST- 2016/11/24 06:00 [entrez]
AID - CPPS-EPUB-79861 [pii]
AID - 10.2174/1389203718666161122105750 [doi]
PST - ppublish
SO  - Curr Protein Pept Sci. 2018;19(1):75-86. doi: 10.2174/1389203718666161122105750.