Zobrazeno 1 - 10
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pro vyhledávání: '"H J, Fromm"'
Autor:
H. J. Fromm
Enzyme kinetics has undergone very rapid growth and development during the past fifteen years and has been well received by the biochemical community. A cursory glance at the current biochem ical literature reveals the increasing popularity of enzy
Publikováno v:
Photochemistry and photobiology. 74(5)
The environment of Trp57, introduced by the mutation of a tyrosine in the dynamic loop of porcine liver fructose-1,6-bisphosphatase (FBPase), was examined using time-resolved fluorescence and directed mutation. The Trp57 enzyme was studied previously
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::359f413365fd5b9160b8eadf98a914e8
https://pubmed.ncbi.nlm.nih.gov/11723795
https://pubmed.ncbi.nlm.nih.gov/11723795
Publikováno v:
Journal of molecular biology. 296(4)
Hexokinase I, the pacemaker of glycolysis in brain tissue, is composed of two structurally similar halves connected by an alpha-helix. The enzyme dimerizes at elevated protein concentrations in solution and in crystal structures; however, almost all
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3fd37f9c8bd9d511af83c2dda8c5df70
https://pubmed.ncbi.nlm.nih.gov/10686099
https://pubmed.ncbi.nlm.nih.gov/10686099
Publikováno v:
Advances in enzymology and related areas of molecular biology. 73
By exerting strategic control on purine nucleotide biosynthesis, and by engaging GTP-dependent transphosphorylation of IMP to activate loss of an oxygen atom during catalysis, adenylosuccinate synthetase remains as enzyme that justifiably fascinates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::42d65cc2daf4d5795980490edb9cdc40
https://pubmed.ncbi.nlm.nih.gov/10218106
https://pubmed.ncbi.nlm.nih.gov/10218106
Publikováno v:
Journal of molecular biology. 282(2)
Hexokinase I, the pacemaker of glycolysis in brain tissue and red blood cells, is comprised of two similar domains fused into a single polypeptide chain. The C-terminal half of hexokinase I is catalytically active, whereas the N-terminal half is nece
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0f76174a62446946f2ff02511d36f42f
https://pubmed.ncbi.nlm.nih.gov/9735292
https://pubmed.ncbi.nlm.nih.gov/9735292
Publikováno v:
The Journal of biological chemistry. 273(26)
On the basis of ligated crystal structures, Asn21, Asn38, Thr42, and Arg419 are not involved in the chemical mechanism of adenylosuccinate synthetase from Escherichia coli, yet these residues are well conserved across species. Purified mutants (Asp21
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::af694acb03eadf4ebc225c72c8e68149
https://pubmed.ncbi.nlm.nih.gov/9632649
https://pubmed.ncbi.nlm.nih.gov/9632649
Autor:
Philippe Chemla, M Girardet, Raymonde Fonne-Pfister, R B Honzatko, E Ward, H J Fromm, K E Kreuz, M G Grütter, Sandra W. Cowan-Jacob, H P Schär
(+)-Hydantocidin, a recently discovered natural spironucleoside with potent herbicidal activity, is shown to be a proherbicide that, after phosphorylation at the 5' position, inhibits adenylosuccinate synthetase, an enzyme involved in de novo purine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::544a5e137ca20e33deac46eeb62b3718
https://europepmc.org/articles/PMC38445/
https://europepmc.org/articles/PMC38445/
Publikováno v:
The Journal of biological chemistry. 271(26)
Structures of adenylosuccinate synthetase from Escherichia coli complexed with guanosine-5'-(beta,gamma-imido) triphosphate and guanosine-5'-(beta,gamma-methylene)triphosphate in the presence and the absence of Mg2+ have been refined to R-factors bel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::63aea48f1c6c18727a436627a8485d80
https://pubmed.ncbi.nlm.nih.gov/8663109
https://pubmed.ncbi.nlm.nih.gov/8663109
Publikováno v:
Biochemistry. 35(23)
The structural transformation of fructose-1,6-bisphosphatase upon binding of the allosteric regulator AMP dramatically changes the interactions across the C1-C4 (C2-C3) subunit interface of the enzyme. Asn9, Met18, and Ser87 residues were modified by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::258ea9507abecce45b417cad81291132
https://pubmed.ncbi.nlm.nih.gov/8652527
https://pubmed.ncbi.nlm.nih.gov/8652527
Autor:
H J, Fromm
Publikováno v:
Methods in enzymology. 249
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3e0a95fa14e57b2dcb4671ecb0be8369
https://pubmed.ncbi.nlm.nih.gov/7791609
https://pubmed.ncbi.nlm.nih.gov/7791609