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- 저자 : Khajamohiddin Syed (검색결과 3 건)
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Khajamohiddin Syed,Karabo Shale,K. H. M. Nazmul Hussain Nazir,Nada Krasevec,Samson Sitheni Mashele,Nataraj Sekhar Pagadala 한국유전학회 2014 Genes & Genomics Vol.36 No.3
Cytochrome P450 monooxygenases (P450s)are ubiquitous heme-thiolate proteins that have potentialbiotechnological application. Thermostable-P450s that canwithstand hostile industrial conditions, such as high temperatures,extremes of pH and organic solvents, are neededfor biotechnological usage. Here, for the first time, wereport a large number of thermostable-P450s from twothermophilic biomass-degrading fungi, Myceliophthorathermophila and Thielavia terrestris. Genome-wide P450analysis revealed the presence of 79 and 70 P450s(P450ome) in T. terrestris and M. thermophila. AuthenticP450s containing both the P450 signature domains (EXXRand CXG) were classified as follows: T. terrestris (50families and 56 subfamilies) and M. thermophila (49families and 53 subfamilies). Bioinformatics analysis ofP450omes suggested the presence of a large number ofthermostable-P450s. Based on aliphatic index cut-off([90), 14 and 11 P450s were determined to be thermostablein T. terrestris and M. thermophila. Among thethermostable P450s, six P450s from T. terrestris and threefrom M. thermophila had a melting temperature (Tm) of[65 C, suggesting their hyperthermal tolerance. Analysisof the instability index of two ascomycete P450omesrevealed the presence of 12 and 19 in vitro stable P450s inT. terrestris and M. thermophila. Overall, six P450s fromT. terrestris and four from M. thermophila showed boththermal tolerance and in vitro stability. Thermophilicascomycetes P450s are of potential interest from a structural,mechanistic and biotechnological point of view, asfive P450s showed higher thermal tolerance and fiveshowed higher in vitro stability compared to the wellcharacterizedthermostable-P450s CYP175A1 (bacteria)and CYP119 (archaea).
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Mthakathi, Ntsane Trevor,Kgosiemang, Ipeleng Kopano Rosinah,Chen, Wanping,Mohlatsane, Molikeng Eric,Mojahi, Thebeyapelo Jacob,Yu, Jae-Hyuk,Mashele, Samson Sitheni,Syed, Khajamohiddin The Korean Society of Phycology 2015 ALGAE Vol.30 No.3
Microalgae research is gaining momentum because of their potential biotechnological applications, including the generation of biofuels. Genome sequencing analysis of two model microalgal species, polar free-living Coccomyxa sp. C-169 and symbiotic Chlorella sp. NC64A, revealed insights into the factors responsible for their lifestyle and unravelled biotechnologically valuable proteins. However, genome sequence analysis under-explored cytochrome P450 monooxygenases (P450s), heme-thiolate proteins ubiquitously present in species belonging to different biological kingdoms. In this study we performed genome data-mining, annotation and comparative analysis of P450s in these two model algal species. Sixty-nine P450s were found in two algal species. Coccomyxa sp. showed 40 P450s and Chlorella sp. showed 29 P450s in their genome. Sixty-eight P450s (>100 amino acid in length) were grouped into 32 P450 families and 46 P450 subfamilies. Among the P450 families, 27 P450 families were novel and not found in other biological kingdoms. The new P450 families are CYP745-CYP747, CYP845-CYP863, and CYP904-CYP908. Five P450 families, CYP51, CYP97, CYP710, CYP745, and CYP746, were commonly found between two algal species and 16 and 11 P450 families were unique to Coccomyxa sp. and Chlorella sp. Synteny analysis and gene-structure analysis revealed P450 duplications in both species. Functional analysis based on homolog P450s suggested that CYP51 and CYP710 family members are involved in membrane ergosterol biosynthesis. CYP55 and CYP97 family members are involved in nitric oxide reduction and biosynthesis of carotenoids. This is the first report on comparative analysis of P450s in the microalgal species Coccomyxa sp. C-169 and Chlorella sp. NC64A.
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Ntsane Trevor Mthakathi,Ipeleng Kopano Rosinah Kgosiemang,Wanping Chen,Molikeng Eric Mohlatsane,Thebeyapelo Jacob Mojahi,Jae-Hyuk Yu,Samson Sitheni Mashele,Khajamohiddin Syed 한국조류학회I 2015 ALGAE Vol.30 No.3
Microalgae research is gaining momentum because of their potential biotechnological applications, including the generation of biofuels. Genome sequencing analysis of two model microalgal species, polar free-living Coccomyxa sp. C-169 and symbiotic Chlorella sp. NC64A, revealed insights into the factors responsible for their lifestyle and unravelled biotechnologically valuable proteins. However, genome sequence analysis under-explored cytochrome P450 monooxygenases (P450s), heme-thiolate proteins ubiquitously present in species belonging to different biological kingdoms. In this study we performed genome data-mining, annotation and comparative analysis of P450s in these two model algal species. Sixty-nine P450s were found in two algal species. Coccomyxa sp. showed 40 P450s and Chlorella sp. showed 29 P450s in their genome. Sixty-eight P450s (>100 amino acid in length) were grouped into 32 P450 families and 46 P450 subfamilies. Among the P450 families, 27 P450 families were novel and not found in other biological kingdoms. The new P450 families are CYP745-CYP747, CYP845-CYP863, and CYP904-CYP908. Five P450 families, CYP51, CYP97, CYP710, CYP745, and CYP746, were commonly found between two algal species and 16 and 11 P450 families were unique to Coccomyxa sp. and Chlorella sp. Synteny analysis and gene-structure analysis revealed P450 duplications in both species. Functional analysis based on homolog P450s suggested that CYP51 and CYP710 family members are involved in membrane ergosterol biosynthesis. CYP55 and CYP97 family members are involved in nitric oxide reduction and biosynthesis of carotenoids. This is the first report on comparative analysis of P450s in the microalgal species Coccomyxa sp. C-169 and Chlorella sp. NC64A.
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