Search results for "norvaline"
showing 4 items of 4 documents
Thymidylate synthases from Hymenolepis diminuta and regenerating rat liver: purification, properties, and inhibition by substrate and cofactor analog…
1995
Comparative studies of thymidylate synthases, isolated from the tapeworm, Hymenolepis diminuta, and regenerating liver of its host, rat, aimed at a possibility of specific inhibition of the helminthic enzyme, are presented. While similar in structure (dimers with monomer molecular masses of 33.7 kDa and 34.9 kDa, respectively) and parameters describing interactions with substrates and products, the tapeworm and rat enzymes differed in the dependences of reaction velocity on temperature (Arrhenius plots biphasic and linear, respectively). The tapeworm, compared with the host, enzyme was less sensitive to the competitive slow-binding inhibition by 5-fluoro-dUMP and its 2-thio congener, but eq…
CCDC 742170: Experimental Crystal Structure Determination
2009
Related Article: C.H.Gorbitz, K.Rissanen, A.Valkonen, A.Husabo|2009|Acta Crystallogr.,Sect.C:Cryst.Struct.Commun.|65|o267|doi:10.1107/S0108270109014309
CCDC 1051240: Experimental Crystal Structure Determination
2015
Related Article: S. Nicholas|2015|Acta Crystallogr.,Sect.E:Cryst.Commun.|71|o216|doi:10.1107/S205698901500393X
Crystal structure of the tripeptideN-(benzyloxycarbonyl)glycylglycyl-L-norvaline
2015
The title tripeptide, C17H23N3O6, contains a nonproteinogenic C-terminal amino acid residue, norvaline, which is an isomer of the amino acid valine. Norvaline, unlike valine, has an unbranched side chain. The molecule has a Gly–Gly segment which adopts an extended conformation. The norvaline residue also adopts an extended backbone conformation while its side chain has ag+tconformation. In the crystal lattice, N—H...O and O—H...O hydrogen bonds stabilize the packing. Molecules translated along the crystallographicaaxis associate through an N—H...O hydrogen bond. The remaining three hydrogen bonds are between molecules related by a21screw axis.