Zobrazeno 1 - 4
of 4
pro vyhledávání: '"R. P. Mellado"'
Publikováno v:
Open Biology, Vol 9, Iss 10 (2019)
Some bacterial peptidyl-prolyl cis/trans isomerases (PPIases) are involved in secretory protein folding after the translocation step. Streptomyces lividans has been used as a host for engineering extracellular overproduction of homologous and heterol
Externí odkaz:
https://doaj.org/article/863a2006924d40fa85eba0fd128559e5
(A) Left: model of mature alpha-amylase with Pro350 residue in cis conformation. Right, model of immature amylase with P350 in trans conformation. The alpha-amylase Pro350 residue has been coloured in red and indicated by a red arrow. The active site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28c9188fbdecc6446405ad5b69bb0d0b
Autor:
V. Parro, R. P. Mellado
Publikováno v:
DNA sequence : the journal of DNA sequencing and mapping. 9(2)
Using synthetic oligonucleotides derived from known signal peptidase genes and a multicopy plasmid as a vector, a signal peptidase gene (sipZ) from Streptomyces lividansTK.21 has been cloned. The primary structure of the gene has been determined and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5efa7bb7741f12c76283456ecb8d12ca
https://pubmed.ncbi.nlm.nih.gov/10520735
https://pubmed.ncbi.nlm.nih.gov/10520735
Publikováno v:
FEMS microbiology letters. 72(2)
Streptomyces lividans grown at 45 degrees C produces a GroEL-like chaperonin. This protein is specifically synthesized in bacterial cell cultures upon heat shock induction. It has a similar size (62 kDa) to the GroEL-like proteins from Escherichia co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f748cefda5f843805899187b85623f1c
https://pubmed.ncbi.nlm.nih.gov/1354626
https://pubmed.ncbi.nlm.nih.gov/1354626