Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Marek Dryjanski"'
Publikováno v:
Chemico-Biological Interactions. :103-114
4-trans-(N,N-dimethylamino)cinnamaldehyde (DACA) is a chromophoric and fluorogenic substrate of aldehyde dehydrogenase. Fluorescence of DACA is enhanced by binding to aldehyde dehydrogenase in the absence of catalysis both in the presence and absence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6aca18a1162f6b01d9e448b2c369d30
https://doi.org/10.1016/s0009-2797(00)00226-x
https://doi.org/10.1016/s0009-2797(00)00226-x
Publikováno v:
European Journal of Biochemistry. 262:704-712
Low concentrations of citral (3,7-dimethyl-2,6-octadienal), an inhibitor of retinoic acid biosynthesis, inhibited E1, E2 and E3 isozymes of human aldehyde dehydrogenase (EC1.2.1.3). The inhibition was reversible on dilution and upon long incubation i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76b59427c6b4b6ba61674f16c3b301d0
https://doi.org/10.1046/j.1432-1327.1999.00415.x
https://doi.org/10.1046/j.1432-1327.1999.00415.x
Publikováno v:
Journal of the American Chemical Society. 118:8207-8212
The hydrolysis of 6-aminopenicillanic acid (APA) at neutral pH, catalyzed by the class C β-lactamase of Enterobacter cloacae P99, was observed from 1H NMR spectra to yield an unexpected product, 8-hydroxypenillic acid, in bicarbonate-containing buff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c423eb942965dbc207ac3e691563fee3
https://doi.org/10.1021/ja961685z
https://doi.org/10.1021/ja961685z
Autor:
Marek Dryjanski, R. F. Pratt
Publikováno v:
Biochemistry. 34:3569-3575
The synthesis of a fluorescent beta-lactamase inhibitor, p-nitrophenyl [(dansylamido)methyl]-phosphonate is described. The compound inactivated the class C beta-lactamase of Enterobacter cloacae P99 with stoichiometric release of p-nitrophenol, presu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::504a0be675c200630fc497d2a79acec7
https://doi.org/10.1021/bi00011a011
https://doi.org/10.1021/bi00011a011
Publikováno v:
Planta. 185:344-349
Metallo-proteinase from 8-d-old seedlings of kale was isolated. The enzyme was extracted with 1% NaCl, concentrated by ammonium sulfate and finally purified by high-performance liquid chromatography. The isolated enzyme had a molecular weight of 22.4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::001ca3fb39b72b57295a8ad7c81009b6
https://doi.org/10.1007/bf00201054
https://doi.org/10.1007/bf00201054
Autor:
Gonzalo Izaguirre, Wojciech Ambroziak, Alexandra Kikonyogo, Darryl P. Abriola, Marek Dryjanski, Regina Pietruszko
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461371465
Aldehyde dehydrogenases catalyze aldehyde dehydrogenation as well as ester hydrolysis. Nitrate esters e.g. isosorbide nitrates and nitroglycerin inhibit the enzyme. Mechanism of inhibition which involves aldehyde dehydrogenase catalyzed formation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eda6148649a08e6aae8167b1c7e7d205
https://doi.org/10.1007/978-1-4615-4735-8_10
https://doi.org/10.1007/978-1-4615-4735-8_10
Publikováno v:
Biochemistry. 37(40)
Human aldehyde dehydrogenase isozymes were inactivated by N-tosyl-L-phenylalanine chloromethyl ketone (TPCK), an inhibitor of chymotrypsin. The inactivation was a first-order process that followed saturation kinetics. NAD and chloral when used togeth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::360fb4431c9710a6e10f85207329edf8
https://pubmed.ncbi.nlm.nih.gov/9760251
https://pubmed.ncbi.nlm.nih.gov/9760251
Publikováno v:
Journal of protein chemistry. 15(7)
Human aldehyde dehydrogenase (EC 1.2.1.3) isozymes E1 and E2 were irreversibly inactivated by stoichiometric concentrations of the haloenol lactones 3-isopropyl-6(E)-bromomethylene tetrahydro-pyran-2-one and 3-phenyl-6(E)-bromomethylene tetrahydropyr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be425d5cdb18457910f2586b51087a17
https://pubmed.ncbi.nlm.nih.gov/8968955
https://pubmed.ncbi.nlm.nih.gov/8968955
Aspartic proteinase from Penicillium camemberti: purification, properties, and substrate specificity
Autor:
Antoni Polanowski, Marek Dryjanski, Maria K. Kołaczkowska, Damian Stachowiak, Józefa Chrzanowska
Publikováno v:
Enzyme and microbial technology. 17(8)
An acid proteinase from the culture filtrate of Penicillium camemberti was isolated in a two-step purification procedure by cation exchange chromatography and gel filtration. The enzyme is an aspartic proteinase inhibited by pepstatin, DAN, and EPNP,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::582053a76547d5330d1b0c04dc28e63c
https://pubmed.ncbi.nlm.nih.gov/7646878
https://pubmed.ncbi.nlm.nih.gov/7646878
Autor:
Marek Dryjanski, R. F. Pratt
Publikováno v:
Biochemistry. 34(11)
Previous research has shown that the class C beta-lactamase of Enterobacter cloacae P99 is able to catalyze the hydrolysis and aminolysis of acyclic depsipeptides. The steady kinetics of these reactions are complicated by the presence of an additiona
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12c8b715c88e1b88d51473cd193a9b9c
https://pubmed.ncbi.nlm.nih.gov/7893652
https://pubmed.ncbi.nlm.nih.gov/7893652