Cytochrome P450, family 105, also known as CYP105, is a cytochrome P450 monooxygenase family in bacteria, predominantly found in the phylum Actinomycetota and the order Actinomycetales. [2] [3] The first three genes and subfamilies identified in this family is the herbicide-inducible P-450SU1 (CYP105A1, subfamily A) and P-450SU2 (CYP105B1, subfamily B) from Streptomyces griseolus [4] [5] and choP (CYP105C1, subfamily C) from Streptomyces sp 's cholesterol oxidase promoter region. [6] [1]
Subfamily [7] | first gene identified | Species | REF |
---|---|---|---|
A | SU1 (CYP105A1) | Streptomyces griseolus | [4] |
B | SU2 (CYP105B1) | Streptomyces griseolus | [4] |
C | choP (CYP105C1) | Streptomyces sp | [6] |
D | soyC (CYP105D1) | Streptomyces griseus | [8] |
E | ORF1 (CYP105E1) | Rhodococcus fascians | [9] |
CYP105 enzymes is widely used in industry, such as the production of pravastatin. [3]
Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Estabrook, Cooper, and Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones.
A tumour inducing (Ti) plasmid is a plasmid found in pathogenic species of Agrobacterium, including A. tumefaciens, A. rhizogenes, A. rubi and A. vitis.
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Cholesterol side-chain cleavage enzyme is commonly referred to as P450scc, where "scc" is an acronym for side-chain cleavage. P450scc is a mitochondrial enzyme that catalyzes conversion of cholesterol to pregnenolone. This is the first reaction in the process of steroidogenesis in all mammalian tissues that specialize in the production of various steroid hormones.
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Iron:rusticyanin reductase is an enzyme with systematic name Fe(II):rusticyanin oxidoreductase. This enzyme catalyses the following chemical reaction
Alcanivorax pacificus is a pyrene-degrading marine gammaproteobacterium. It is of the genus Alcanivorax, a group of marine bacteria known for degrading hydrocarbons. When originally proposed, the genus Alcanivorax comprised six distinguishable species. However, A. pacificus, a seventh strain, was isolated from deep sea sediments in the West Pacific Ocean by Shanghai Majorbio Bio-pharm Technology Co., Ltd. in 2011. A. pacificus’s ability to degrade hydrocarbons can be employed for cleaning up oil-contaminated oceans through bioremediation. The genomic differences present in this strain of Alcanivorax that distinguish it from the original consortium are important to understand to better utilize this bacteria for bioremediation.
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Catherine Louise Kearney Squires was a microbiologist known for her work on ribosomal RNA using Escherichia coli as a model organism. She was an elected fellow of the American Academy of Microbiology and the American Association for the Advancement of Science.
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