Valine biochemical structure

HRV Arnstein, D Morris. The structure of a peptide, containing alpha-aminoadipic acid, cysteine and valine, present in the mycelium of Penicillium chrysogenum. Biochem J 76 357-361, 1960. 

JE Baldwin, C-Y Shiau, MF Byford, CJ Schofield. Substrate specificity of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine formed by ACV synthetase from Cephalosporium acremonium. demonstration of the structure of several unnatural tripeptide products. Biochem J 301 367-372, 1994. 

Figure 2 Order and organization of enniatin synthetase and cyclosporin synthetase as deduced from gene sequence and biochemical characterization. Symbols in the adenylateforming modules (black boxes) indicate the corresponding activated amino acids. M stands for A -methyltransferase domain. Condensation domains are represented by white boxes. (A) Top Structure of enniatin synthetase. EA represents the D-Hiv-activating module EB represents the L-valine-activating module D-Ehv is D-2-hydroxyisovaleric acid. Bottom Structural features of the wild-type A -methyltransferase domain M of esynl. The black boxes indicate conserved motifs which can be found within methyltransferases and A -methyltransferase domains of peptide synthetases (see also Fig. 3). The numbers indicate the amino acid position in the sequence of Esyn. (B) Structure of cyclosporin synthetase. Abu = L-a-aminobutyric acid Bmt = (4A)-4-[(E)-2-butenyl]-4-methyl-L-threonine.

Draw the chemical structures of PTC-valine and PTH-valine. With what biochemical technique is the formation of PTH-amino acid derivatives associated ... 

Branched-chain ketoaciduria (commonly known as Maple Syrup Urine Disease MSUD) is another ailment that may be caused by thiamine deficiency. In MSUD, the oxidative decarboxylation of alpha-keto acids derived from, i.e. valine, isoleucine, and leucine, is blocked due to an inadequate supply of the coenzyme thiamine pyrophosphate (TPP). Clinical symptoms of MSUD include mental and physical retardation. Describe briefly the structure of Riboflavin (Vitamin B-2) and its biochemical role. 

Normal hemoglobin (HbA) is composed of two a chains and two chains (a2/S2)- The biochemical defect that leads to the development of HbS involves the substitution of valine for glutamic acid as the sixth amino acid in the /3-polypeptide chain. Another type of abnormal hemoglobin, hemoglobin C (HbC), is produced by the substitution of lysine for glutamic acid as the sixth amino acid in the 8-chain. Structurally, the a-chains of HbS, HbA, and HbC are identical. Therefore it is the chemical differences in the /3-chain that explain sickling and its related sequelae. ... 

Arnstein, H. R. V., and D. Morris The Structure of a Peptide Containing a-Aminoadipic Acid, Cystine and Valine, Present in the Mycelium of Penicillium chrysogenum. Biochem. J. 76, 357 (1960). 

Sarges, R., and B. Witkop Gramicidin VIII. The structure of valine- and isoleucine-gramicidin C. Biochem. 4, 2491 (1965 a). 

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