Zobrazeno 1 - 10
of 28
pro vyhledávání: '"M F, Dunn"'
Autor:
M. F. Dunn
Publikováno v:
The handbook of microbial metabolism of amino acids
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa4290947e5a69b06bf5196606960b59
https://doi.org/10.1079/9781780647234.0352
https://doi.org/10.1079/9781780647234.0352
Autor:
A. Hickman, M. F. Dunn, Munirathiram Sundaramoorthy, E. Woehl, Thomas L. Poulos, Kalidip Choudhury, T. Yonetani
Publikováno v:
Journal of Biological Chemistry. 269:20239-20249
The role of the proximal histidine ligand in peroxidase function was studied by replacing the His side chain in cytochrome c peroxidase with Gln, Glu, or Cys. In addition, a double mutant was prepared where His-175 is converted to Gln and the site of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a639f410e0105041196ad2fe51a5ff04
https://doi.org/10.1016/s0021-9258(17)31982-8
https://doi.org/10.1016/s0021-9258(17)31982-8
Publikováno v:
Biochemistry. 38(22)
The alpha-subunit of the tryptophan synthase bienzyme complex catalyzes the formation of indole from the cleavage of 3-indolyl-D-glyceraldehyde 3'-phosphate, while the beta-subunit utilizes L-serine and the indole produced at the alpha-site to form t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b422358760407f715965b1ff28ac6312
https://pubmed.ncbi.nlm.nih.gov/10353823
https://pubmed.ncbi.nlm.nih.gov/10353823
Publikováno v:
The Journal of biological chemistry. 272(2)
Magnetic circular dichroism (MCD) spectra of a series of adducts formed by the Co(II)-substituted R-state insulin hexamer are reported. The His-B10 residues in this hexamer form tris imidazole chelates in which pseudotetrahedral Co(II) centers are co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cabed0c4419ff0151670e34511ec6c90
https://pubmed.ncbi.nlm.nih.gov/8995407
https://pubmed.ncbi.nlm.nih.gov/8995407
Publikováno v:
Proteins. 26(4)
The insulin hexamer is an allosteric protein exhibiting both positive and negative cooperative homotropic interactions and positive cooperative heterotropic interactions (C. R. Bloom et al., J. Mol. Biol. 245, 324-330, 1995). In this study, detailed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d9b4bec746c73b1a269926636cf4ecbf
https://pubmed.ncbi.nlm.nih.gov/8990494
https://pubmed.ncbi.nlm.nih.gov/8990494
Autor:
P S, Brzović, M F, Dunn
Publikováno v:
Methods in enzymology. 246
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::204e378448380dfd652c3f05510cd54d
https://pubmed.ncbi.nlm.nih.gov/7752924
https://pubmed.ncbi.nlm.nih.gov/7752924
Publikováno v:
The Journal of biological chemistry. 269(32)
The role of the proximal histidine ligand in peroxidase function was studied by replacing the His side chain in cytochrome c peroxidase with Gln, Glu, or Cys. In addition, a double mutant was prepared where His-175 is converted to Gln and the site of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::476a4a0b34cb22d155924c6990f04866
https://pubmed.ncbi.nlm.nih.gov/8051115
https://pubmed.ncbi.nlm.nih.gov/8051115
Autor:
P S, Brzović, M F, Dunn
Publikováno v:
Methods of biochemical analysis. 37
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::73dfd07c3f34df0b742a0447170f0bba
https://pubmed.ncbi.nlm.nih.gov/8309367
https://pubmed.ncbi.nlm.nih.gov/8309367
Publikováno v:
The Journal of biological chemistry. 268(2)
Human liver alcohol dehydrogenase isoenzymes beta 1 beta 1 and beta 2 beta 2, in which position 47 in the coenzyme binding domain is an arginine or histidine, respectively, differ remarkably in steady-state kinetics. To understand which catalytic ste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::20eaab27ac201cde768e107f3333c76d
https://pubmed.ncbi.nlm.nih.gov/8419368
https://pubmed.ncbi.nlm.nih.gov/8419368
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461362593
Ethanol and other alcohols are metabolized in liver by alcohol dehydrogenase isoenzymes. At least five electrophoretically distinct isoenzymes are found in human liver that can be divided into three classes (Burnell & Bosron, 1989). Class I comprises
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e47f9b44a41d8d7000e4cadc33243a1
https://doi.org/10.1007/978-1-4615-2904-0_45
https://doi.org/10.1007/978-1-4615-2904-0_45