Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Matthew B. Tobin"'
Autor:
Keith A., Powell, Sandra W., Ramer, Stephen B., Del Cardayré, Willem P. C., Stemmer, Matthew B., Tobin, Pascal F., Longchamp, Gjalt W., Huisman
Publikováno v:
Angewandte Chemie (International ed. in English). 40(21)
This review describes the current state of biocatalysis in the chemical industry. Although we recognize the advantages of chemical approaches, we suggest that the use of biological catalysis is about to expand dramatically because of the recent devel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0ca8212fb0306497da4de699fd6c82c9
https://pubmed.ncbi.nlm.nih.gov/12404465
https://pubmed.ncbi.nlm.nih.gov/12404465
Autor:
James R. Miller, Jack E. Baldwin, Matthew B. Tobin, John D. Sutherland, Stephen C.J. Cole, Steven Kovacevic
Publikováno v:
FEMS microbiology letters. 121(1)
Using a high level Escherichia coli expression system for the Penicillium chrysogenum penDE gene, we have produced acyl-coenzyme A: isopenicillin N acyltransferase (AT) enzymes containing amino acid substitutions at three conserved Ser residues. Chos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc792d38261baade04bcf0585e88882b
https://pubmed.ncbi.nlm.nih.gov/8082826
https://pubmed.ncbi.nlm.nih.gov/8082826
Publikováno v:
FEBS letters. 319(1-2)
A high level E. coli expression system has been constructed for the Penicillium chrysogenum penDE gene, which encodes the acyl-coenzyme A: isopenicillin N-acyltransferase (AT) enzyme. Induction of overexpression of recombinant AT (recAT) by increasin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a9f236379b30e68b88550777ba5ab17
https://pubmed.ncbi.nlm.nih.gov/8384123
https://pubmed.ncbi.nlm.nih.gov/8384123