Glycine biochemical structure

Yano, M., Nagai, K., Morimoto, K., and Miyamoto, H. (2007) Shematrin a family of glycine-rich structural proteins in the shell of the pearl oyster Pinctada Jucata. Comp. Biochem. Physiol., 144B, 254-262. 

Lindermayr, C. et al.. Divergent members of a soybean Glycine max L.) 4-coumarate coenzyme A ligase gene family — primary structures, catalytic properties, and differential expression. Eur. J. Biochem., 269, 1304, 2002. 

Yoshida, K. et al., Structural analysis and measurement of anthocyanins from colored seed coats of Vigna, Phaseolus, and Glycine legumes, Biosci. Biotechnol. Biochem., 60, 589, 1996. 

The receptors for acetylcholine, GABA, glycine and serotonin have a homologous structure and form a superfamily. The best-investigated representative of this superfamUy is the nicotinic acetylcholine receptor, for which extensive biochemical and structural data are available. The nicotinic acetylcholine receptor can be treated as a representative of the other receptors of the superfamUy since it can be assumed that the structure-function principles of this receptor apply to the others. 

Shutov, A.D., Kakhovskaya, I.A., Bastrygina, A.S., Bulmaga, V.P, Horstmann, C., Muntz, K. 1996. Limited proteolysis of P-conglycinin and glycinin, the 7s and 11s storage globulins from soybean (Glycine max (L.) Merr.) Structural and evolutionary implications. Eur J Biochem 241 221-228. 

Copper is often found in biochemical systems, usually in peptides and proteins. Extensive reviews may be found (66, 106, 557). Semiquantita-tive discussion (112) of the significance of the results, which usually show that the copper environment has axial symmetry and with a distorted octahedral structure are numerous. The use of model compounds has been discussed by Malmstrom and Vanngard (477). In many cases there appears to be dimeric species present (9S). A system of importance which has been extensively studied is the series of complexes with glycine and triglycine (209, 638, 707, 712). The ESR data are tabulated in Table LV. 

The outlines of the biosynthetic pathway of the complicated porphyrin structure have been established through elegant use of isotopic methods and biochemical genetics and several of the intermediates have been established, but the details of the enzymatic reactions are only now being investigated. The atoms of porphyrins are all derived from active succinate and glycine.These condense to form a-amino-j8-ketoadipic acid. The decarboxylation of this /3-keto acid results in the formation of... 

All proteins are synthesized from the 20 a-amino acids specified by the genetic code as shown in Fig. 1. The nature of an amino acid is determined by the side-chain attached to the a-carbon (Table I). All of these amino acids, except for glycine which carries two hydrogens on its a-carbon, have a chiral center located at the a-carbon. Thus the amino acids exist as either the l- or D-isomers. Only the L-stereoisomer is utilized in protein biosynthesis (Fig. 2). This introduces chirality into all protein molecules that is the source of most of the asymmetric features found in protein structures. The use of only one of the two stereoisomers of the amino acids also establishes a structural uniqueness that is essential for biochemical specificity. 

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