Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Arie de Kok"'
Publikováno v:
European Journal of Biochemistry. 106:49-58
The 2-oxoglutarate dehydrogenase complex from Acetobacter xylinum consists of three components, 2-oxoglutarate dehydrogenase (E1), lipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). The molecular weight of the complex as studied by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bcf80e20c74aaab90262efb48cce3e6
https://doi.org/10.1111/j.1432-1033.1980.tb05996.x
https://doi.org/10.1111/j.1432-1033.1980.tb05996.x
Autor:
Nicole Dieteren, David Arscott, Jacques A.E. Benen, Cees Veeger, Arie de Kok, Willem J. H. van Berkel, Charles H. Williams
Publikováno v:
European Journal of Biochemistry. 207:487-497
Three amino acid residues in the active site of lipoamide dehydrogenase from Azotobacter vinelandii were replaced with other residues. His450, the active-site base, was replaced with Ser, Tyr or Phe. Pro451, from X-ray analysis found to be in cis con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c538644b31d96a8595f754f767750bf
https://doi.org/10.1111/j.1432-1033.1992.tb17075.x
https://doi.org/10.1111/j.1432-1033.1992.tb17075.x
Publikováno v:
European Journal of Biochemistry, 206, 427-435
European Journal of Biochemistry 206 (1992)
European Journal of Biochemistry 206 (1992)
Two unique restriction sites were introduced by site-directed mutagenesis at identical positions in the DNA encoding the dihydrolipoyltransacetylase (E2p) components of the pyruvate dehydrogenase complex from Azotobacter vinelandii and from Escherich
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30989e3007dd4d752020f00d514a5943
https://doi.org/10.1111/j.1432-1033.1992.tb16943.x
https://doi.org/10.1111/j.1432-1033.1992.tb16943.x
Publikováno v:
European Journal of Biochemistry. 202:1049-1055
The conformational stability of holo-lipoamide and apo-lipoamide dehydrogenase from Azotobacter vinelandii was studied by thermoinactivation, unfolding and limited proteolysis. The oxidized holoenzyme is thermostable, showing a melting temperature, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::428c88aa5d90319fa5ba616e3942ca2d
https://doi.org/10.1111/j.1432-1033.1991.tb16469.x
https://doi.org/10.1111/j.1432-1033.1991.tb16469.x
Publikováno v:
Protein Science. 6:913-915
Members of the family of 2-oxoacid dehydrogenase multienzyme complexes catalyze the oxidative decarboxylation of alpha-keto acids and are among the most remarkable enzymatic machineries in the living cell. These multienzyme complexes combine a highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1f9f47d9f7a6e8cc4925de648c565fe
https://doi.org/10.1002/pro.5560060419
https://doi.org/10.1002/pro.5560060419
Engineering of microheterogeneity-resistantp-hydroxybenzoate hydroxylase fromPseudomonas fluorescens
Autor:
Kor H. Kalk, Wim G. J. Hol, Galina Obmolova, Arie de Kok, Klaus Eschrich, Willem J. H. van Berkel, Andrea Mattevi, Adrie H. Westphal
Publikováno v:
FEBS Letters. 277:197-199
By site-directed mutagenesis, Cys-116 was converted to Ser-116 in p-hydroxybenzoate hydroxylase (EC 1.14.13.2) from Pseudomonas fluorescens. In contrast to wild-type enzyme, the C116S mutant is no longer susceptible to oxidation by hydrogen peroxide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a94db1cd0c6108057c2d7520c3c97025
https://doi.org/10.1016/0014-5793(90)80843-8
https://doi.org/10.1016/0014-5793(90)80843-8
Autor:
Adrie H. Westphal, Jacky L. Snoep, Mark R. de Graef, Oense M. Neijssel, M. Joost Teixeira de Mattos, Arie de Kok
Publikováno v:
FEMS microbiology letters. 114(3)
The effect of NADH on the activity of the purified pyruvate dehydrogenase complexes (PDHc) of Enterococcus (Ec.) faecalis, Lactococcus lactis, Azotobacter vinelandii and Escherichia coli was determined in vitro. It was found that the PDHc of E. coli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a3ad77c8224fb22afd01ebaa31690a0
https://pubmed.ncbi.nlm.nih.gov/8288104
https://pubmed.ncbi.nlm.nih.gov/8288104
Publikováno v:
European journal of biochemistry. 210(2)
The gene encoding p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens was cloned in Escherichia coli to provide DNA for mutagenesis studies on the protein product. A plasmid containing a 1.65-kbp insert of P. fluorescens chromosomal DNA was ob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a6dfb5477386651877770342908ad70
https://pubmed.ncbi.nlm.nih.gov/1459126
https://pubmed.ncbi.nlm.nih.gov/1459126
Publikováno v:
European journal of biochemistry. 187(1)
The nucleotide sequence encoding the succinyltransferase component (E2o) of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii has been determined. Previously the cloning in Escherichia coli of the gene encoding lipoamide dehydrogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::beacf011da8566422dda921ae518a782
https://pubmed.ncbi.nlm.nih.gov/2404759
https://pubmed.ncbi.nlm.nih.gov/2404759
Publikováno v:
FEBS Letters. 240:205-210
600 MHz 1H-NMR spectroscopy demonstrates that the pyruvate dehydrogenase complex of Azotobacter vinelandii contains regions of the polypeptide chain with intramolecular mobility. This mobility is located in the E2 component and can probably be ascrib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::201432a9a9475737727bbc5c8160a98f
https://doi.org/10.1016/0014-5793(88)80369-7
https://doi.org/10.1016/0014-5793(88)80369-7