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Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity
Wu, Xiao-Bin1; Tian, Xiu-Yun1; Ji, Jun-Jie1; Wu, Wei-Bin1; Fan, Ke-Qiang1,2; Yang, Ke-Qian1; Yang, KQ
2011-04-01
Source PublicationBIOTECHNOLOGY LETTERS
ISSN0141-5492
Volume33Issue:4Pages:805-812
AbstractDeacetoxy/deacetylcephalosporin C synthase (acDAOC/DACS) from Acremonium chrysogenum is a bifunctional enzyme that catalyzes both the ring-expansion of penicillin N to deacetoxycephalosporin C and the hydroxylation of the latter to deacetylcephalosporin C. The R308 residue located in close proximity to the C-terminus of acDAOC/DACS was mutated to the other 19 amino acids. In the resulting mutant pool, R308L, R308I, R308T and R308V showed significant improvement in their ability to convert penicillin analogs, thus confirming the role of R308 in controlling substrate selectivity, the four amino acids all possess short aliphatic sidechains that may improve hydrophobic interactions with the substrates. The mutant R308I showed the highest reactivity for penicillin G, with 3-fold increase in k(cat)/K(m) ratio and 7-fold increase in relative activity.
KeywordAcremonium Chrysogenum C-terminus Expandase Kinetics Mutagenesis
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1007/s10529-010-0504-5
Indexed BySCI
Language英语
WOS KeywordRING-EXPANSION ACTIVITY ; AMINO-ACID ALTERATIONS ; PENICILLIN-G ; COMPLETE LIBRARY ; CATALYSIS ; TERMINUS ; BINDING ; CONVERSION ; MUTATIONS ; ENZYME
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
WOS IDWOS:000288548900023
Citation statistics
Cited Times:6[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/5071
Collection生化工程国家重点实验室
Corresponding AuthorYang, KQ
Affiliation1.Chinese Acad Sci, State Key Lab Microbial Resources, Inst Microbiol, Beijing 100190, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Wu, Xiao-Bin,Tian, Xiu-Yun,Ji, Jun-Jie,et al. Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity[J]. BIOTECHNOLOGY LETTERS,2011,33(4):805-812.
APA Wu, Xiao-Bin.,Tian, Xiu-Yun.,Ji, Jun-Jie.,Wu, Wei-Bin.,Fan, Ke-Qiang.,...&Yang, KQ.(2011).Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity.BIOTECHNOLOGY LETTERS,33(4),805-812.
MLA Wu, Xiao-Bin,et al."Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity".BIOTECHNOLOGY LETTERS 33.4(2011):805-812.
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