Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Gitte Meriläinen"'
Publikováno v:
Protein Science. 25:987-998
The type III secretion system (T3SS) is required for the virulence of many gram-negative bacterial human pathogens. It is composed of several structural proteins, forming the secretion needle and its basis, the basal body. In Chlamydia spp., the T3SS
Autor:
Gitte Meriläinen, Rik K. Wierenga
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 70:1431-1433
The inner membrane ring of the bacterial type III secretion system (TTSS) is composed of two proteins. InChlamydia trachomatisthis ring is formed by CdsD (gene nameCT_664) and CdsJ (gene nameCTA_0609). CdsD consists of 829 amino acids. The last 400 a
Publikováno v:
Biochemistry. 48:11011-11025
The biosynthetic thiolase catalyzes a Claisen condensation reaction between acetyl-CoA and the enzyme acetylated at Cys89. Two oxyanion holes facilitate this catalysis: oxyanion hole I stabilizes the enolate intermediate generated from acetyl-CoA, wh
Publikováno v:
FEBS Journal. 275:6136-6148
Thioesters are more reactive than oxoesters, and thioester chemistry is important for the reaction mechanisms of many enzymes, including the members of the thiolase superfamily, which play roles in both degradative and biosynthetic pathways. In the r
Autor:
Toshiyuki Fukao, Gitte Meriläinen, Naomi Kondo, Päivi Pirilä, Rik K. Wierenga, Antti M. Haapalainen
Publikováno v:
Biochemistry. 46:4305-4321
Thiolases are CoA-dependent enzymes which catalyze the formation of a carbon-carbon bond in a Claisen condensation step and its reverse reaction via a thiolytic degradation mechanism. Mitochondrial acetoacetyl-coenzyme A (CoA) thiolase (T2) is import
Publikováno v:
Trends in Biochemical Sciences. 31:64-71
The formation of a carbon-carbon bond is an essential step in the biosynthetic pathways by which fatty acids and polyketides are made. The thiolase superfamily enzymes catalyse this carbon-carbon-bond formation via a thioester-dependent Claisen-conde
Autor:
Gitte Meriläinen, Kristoffer Brännström, Shenghua Huang, Tobias Hainzl, A. Elisabeth Sauer-Eriksson
Publikováno v:
Nature Structural & Molecular Biology. 18:389-391
The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-Å structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural
Autor:
Gitte Meriläinen, Tuomo Glumoff, J.E Jalonen, R.K. Wierenga, Päivi Pirilä, Antti M. Haapalainen, J.K. Hiltunen, D.M.F. van Aalten
Publikováno v:
Journal of Molecular Biology. 313:1127-1138
β-Oxidation of amino acyl coenzyme A (acyl-CoA) species in mammalian peroxisomes can occur via either multifunctional enzyme type 1 (MFE-1) or type 2 (MFE-2), both of which catalyze the hydration of trans -2-enoyl-CoA and the dehydrogenation of 3-hy
Publikováno v:
The FEBS journal. 275(24)
Thioesters are more reactive than oxoesters, and thioester chemistry is important for the reaction mechanisms of many enzymes, including the members of the thiolase superfamily, which play roles in both degradative and biosynthetic pathways. In the r