Výsledky vyhledávání - "R K, Wierenga"

Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution

Autor: A M, Haapalainen, D M, van Aalten, G, Meriläinen, J E, Jalonen, P, Pirilä, R K, Wierenga, J K, Hiltunen, T, Glumoff

Publikováno v: Journal of molecular biology. 313(5)

beta-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-h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::45ee2838072de259d23407112f3d5d24
https://pubmed.ncbi.nlm.nih.gov/11700068

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Structural determinants for ligand binding and catalysis of triosephosphate isomerase

Autor: I, Kursula, S, Partanen, A M, Lambeir, D M, Antonov, K, Augustyns, R K, Wierenga

Publikováno v: European journal of biochemistry. 268(19)

The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis. IPP is an analogue of the substrate D-glyceraldehyde-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c493df54dba34f8ee2009839a41e2934
https://pubmed.ncbi.nlm.nih.gov/11589711

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The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase

Autor: A M, Mursula, D M, van Aalten, J K, Hiltunen, R K, Wierenga

Publikováno v: Journal of molecular biology. 309(4)

The active-site geometry of the first crystal structure of a Delta(3)-Delta(2)-enoyl-coenzyme A (CoA) isomerase (the peroxisomal enzyme from the yeast Saccharomyces cerevisiae) shows that only one catalytic base, Glu158, is involved in shuttling the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0e6a458bad6b3b6ebb230c4eaa021068
https://pubmed.ncbi.nlm.nih.gov/11399063

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Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity

Autor: B V, Norledge, A M, Lambeir, R A, Abagyan, A, Rottmann, A M, Fernandez, V V, Filimonov, M G, Peter, R K, Wierenga

Publikováno v: Proteins. 42(3)

Loop 8 (residues 232-242) in triosephosphate isomerase (TIM) is a highly conserved loop that forms a tight binding pocket for the phosphate moiety of the substrate. Its sequence includes the fully conserved, solvent-exposed Leu238. The tight phosphat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7d750305b45f45f2026be11e74fafcc5
https://pubmed.ncbi.nlm.nih.gov/11151009

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Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase

Autor: Y, Modis, R K, Wierenga

Publikováno v: Journal of molecular biology. 297(5)

Biosynthetic thiolases catalyze the biological Claisen condensation of two acetyl-CoA molecules to form acetoacetyl-CoA. This is one of the fundamental categories of carbon skeletal assembly patterns in biological systems and is the first step in man

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b670930c3c57fc9fd2365254ca4dcdc7
https://pubmed.ncbi.nlm.nih.gov/10764581

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The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule

Autor: C K, Engel, T R, Kiema, J K, Hiltunen, R K, Wierenga

Publikováno v: Journal of molecular biology. 275(5)

The structure of the hexameric rat mitochondrial enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA, has been refined at a resolution of 2.4 A. Enoyl-CoA hydratase catalyses the hydration of 2,3-unsaturated enoyl-CoA th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3be1df665075a49ecc6bb7d4ee395c6c
https://pubmed.ncbi.nlm.nih.gov/9480773

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Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties

Autor: M, Alvarez, J P, Zeelen, V, Mainfroid, F, Rentier-Delrue, J A, Martial, L, Wyns, R K, Wierenga, D, Maes

Publikováno v: The Journal of biological chemistry. 273(4)

The purification and characterization of triose-phosphate isomerase from the psychrophilic bacterium Vibrio marinus (vTIM) is described. Crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex (at a 2.7-A resolution) ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::94653412084f488cb3082abfcedb378b
https://pubmed.ncbi.nlm.nih.gov/9442062

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Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket

Autor: C K, Engel, M, Mathieu, J P, Zeelen, J K, Hiltunen, R K, Wierenga

Publikováno v: The EMBO journal. 15(19)

The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme catalyses the reversible addition of water to alpha,beta-u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::405ebbfc07f25c0bae8a18bc5e6f6cf7
https://pubmed.ncbi.nlm.nih.gov/8895557

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The 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha structure constructed from two core domains of identical topology

Autor: M, Mathieu, J P, Zeelen, R A, Pauptit, R, Erdmann, W H, Kunau, R K, Wierenga

Publikováno v: Structure (London, England : 1993). 2(9)

The peroxisomal enzyme 3-ketoacyl-coenzyme A thiolase of the yeast Saccharomyces cerevisiae is a homodimer with 417 residues per subunit. It is synthesized in the cytosol and subsequently imported into the peroxisome where it catalyzes the last step

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::915b1c3babaf8115924c1940ed0a4e0a
https://pubmed.ncbi.nlm.nih.gov/7812714

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