Zobrazeno 1 - 10
of 103
pro vyhledávání: '"Johan N. Jansonius"'
The aspartate and tyrosine aminotransferases from Escherichia coli have 43% sequence identity and nearly identical active sites. Both are equally good enzymes for dicarboxylate substrates, but the latter transaminates aromatic amino acids 1000 times
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8014f02855c189f74ff4cef3c163c19
http://doc.rero.ch/record/302853/files/7-5-605.pdf
http://doc.rero.ch/record/302853/files/7-5-605.pdf
Publikováno v:
Journal of Molecular Biology. 319:757-766
Indoleglycerol phosphate synthase catalyzes the ring closure of an N-alkylated anthranilate to a 3-alkyl indole derivative, a reaction requiring Lewis acid catalysis in vitro. Here, we investigated the enzymatic reaction mechanism through X-ray cryst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f279768f3c5418eb6f40eb4255619b3e
https://doi.org/10.1016/s0022-2836(02)00378-9
https://doi.org/10.1016/s0022-2836(02)00378-9
Publikováno v:
Journal of Biological Chemistry. 277:8626-8634
The crystal structure of the thermostable indoleglycerol-phosphate synthase from Thermotoga maritima(tIGPS) was determined at 2.5 A resolution. It was compared with the structures of the thermostable sIGPS from Sulfolobus solfataricus and of the ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40b7562b0c69b8c12ef8e29f2767ea54
https://doi.org/10.1074/jbc.m109517200
https://doi.org/10.1074/jbc.m109517200
Autor:
Vladimir N. Malashkevich, Paola Dominici, Peter Burkhard, Carla Borri-Voltattorni, Johan N. Jansonius
Publikováno v:
Nature Structural Biology. 8:963-967
DOPA decarboxylase (DDC) is responsible for the synthesis of the key neurotransmitters dopamine and serotonin via decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) and L-5-hydroxytryptophan, respectively. DDC has been implicated in a number of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fff04a3caa714b136e70199726155e5c
https://doi.org/10.1038/nsb1101-963
https://doi.org/10.1038/nsb1101-963
Publikováno v:
Journal of Molecular Biology. 303:279-286
A new crystal structure of O-acetylserine sulfhydrylase (OASS) has been solved with chloride bound at an allosteric site and sulfate bound at the active site. The bound anions result in a new “inhibited” conformation, that differs from the “ope
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb60f1ee54d4fb689a039e44d937f109
https://doi.org/10.1006/jmbi.2000.4109
https://doi.org/10.1006/jmbi.2000.4109
Autor:
Zora Marković-Housley, Guido Capitani, G. DelVal, Peter Schürmann, Johan N. Jansonius, M. Morris
Publikováno v:
Journal of Molecular Biology. 302:135-154
Thioredoxins are small ubiquitous proteins which act as general protein disulfide reductases in living cells. Chloroplasts contain two distinct thioredoxins ( f and m) with different phylogenetic origin. Both act as enzyme regulatory proteins but hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70649776ea689acbc72f7941bfa95b8f
https://doi.org/10.1006/jmbi.2000.4006
https://doi.org/10.1006/jmbi.2000.4006
Autor:
Liang Feng, Paola Storici, Guido Capitani, Johan N. Jansonius, Erhard Hohenester, Jack F. Kirsch
Publikováno v:
Journal of Molecular Biology. 294:745-756
The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2458588a6e9ac7c33241ab489a5faea
https://doi.org/10.1006/jmbi.1999.3255
https://doi.org/10.1006/jmbi.1999.3255
Publikováno v:
Journal of Molecular Biology. 294:193-200
The crystal structures of four inhibitor complexes of dialkylglycine decarboxylase are reported. The enzyme does not undergo a domain closure, as does aspartate aminotransferase, upon inhibitor binding. Two active-site conformations have been observe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::88c0ba06f0b74c6cc1bc26cfcbf54110
https://doi.org/10.1006/jmbi.1999.3254
https://doi.org/10.1006/jmbi.1999.3254
Publikováno v:
Journal of Molecular Biology. 291:941-953
Covalent binding of L-methionine as an external aldimine to the pyridoxal 5'-phosphate-cofactor in the K41A mutant of O-acetylserine sulfhydrylase from Salmonella typhimurium induces a large conformational change in the protein. Methionine mimics the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a621592fd582a54c1bbdfc925e49911d
https://doi.org/10.1006/jmbi.1999.3002
https://doi.org/10.1006/jmbi.1999.3002
Publikováno v:
Journal of Molecular Biology. 288:753-763
The recombinantly expressed protein indoleglycerol phosphate synthase from the hyperthermophilic bacterium Thermotoga maritima (tIGPS) was purified and characterized with respect to oligomerization state, catalytic properties and thermostability. Thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b6af3f3ae2dba34e1b2fda5055d8d5f
https://doi.org/10.1006/jmbi.1999.2709
https://doi.org/10.1006/jmbi.1999.2709