Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity

Biotechnology Letters

Volumn 33, Issue 4, 2011, Pages 805-812

  Wu, Xiao Bin ^a   Tian, Xiu Yun ^a   Ji, Jun Jie ^a   Wu, Wei Bin ^a   Fan, Ke Qiang ^a,b   Yang, Ke Qian ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

^b INSTITUTE OF PROCESS ENGINEERING   (China)

Author keywords

Acremonium chrysogenum; C terminus; Expandase; Kinetics; Mutagenesis

Indexed keywords

ACREMONIUM; BIFUNCTIONAL ENZYMES; C-TERMINUS; CLOSE PROXIMITY; EXPANDASE; FOUR AMINO ACIDS; HYDROPHOBIC INTERACTIONS; PENICILLIN G; RELATIVE ACTIVITIES; SATURATION MUTAGENESIS; SIDE CHAINS; SUBSTRATE SELECTIVITY; SUBSTRATE SPECIFICITY; SYNTHASES;

AMINO ACIDS; HYDROPHOBICITY; LAKES; MUTAGENESIS; SUBSTRATES;

DRUG PRODUCTS;

DESACETOXYCEPHALOSPORIN C SYNTHETASE; DRUG DERIVATIVE; OXIDOREDUCTASE; PENICILLIN G;

ACREMONIUM; ARTICLE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MUTAGENESIS; MUTATION;

ACREMONIUM; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; MUTAGENESIS; MUTATION; OXIDOREDUCTASES; PENICILLIN G; SUBSTRATE SPECIFICITY;

ACREMONIUM CHRYSOGENUM;

EID: 79952774379     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-010-0504-5     Document Type: Article

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