Arginine biochemical structure

The mechanism that is consistent with biochemical, enzymological and structural data involves binding of arginine, in which the side-chain of Glu277 plays an important role, attack of the nucleophilic metal-bridged hydroxyl ion, formation of a neutral, tetrahedral intermediate which is stabilized by the dinuclear Mn(II) centre, and finally proton transfer from Hisl41, followed by release of the two products (Figure 16.5). 

Regnouf, E Kassab, R. Fattoum, A. Primary structure of lobster-muscle arginine kinase. Isolation and characterization of the fragments produced by cyanogen-bromide cleavage. Eur. J. Biochem., 44, 67-79 (1974)... 

Robin, Y. Guillou, A. Thoai, N.V. Unspecific arginine kinase of molecular weight 150 000. Amino acid composition, subunit structure and number of substrate binding sites. Eur. J. Biochem., 52, 531-537 (1975)... 

Lin, Q. and Brookes, P. C. (1999b). Arginine ammonification as a method to estimate soil microbial biomass and microbial community structure. Soil Biol. Biochem. 31,1985-1997. 

The structure of the bacterial ArsC from Escherichia coli plasmid R773 has been solved at 1.65 A resolution, and revealed that arsenate reductase (ArsC) has only one cysteine residue (Cys-12) in the active site, surrounded by an arginine triad composed of Arg-60, Arg-94, and Arg-107 (Mukhopadhyay et al, 2002). However, the arsenate reductase from Staphylococcus aureus has three cysteine residues (Cys-10, Cys-82, and Cys-89). The biochemical and mutational studies established that the arsenate binds to the triad of arginine (Arg-60, Arg-94, and Arg-107) residues and forms a covalent bond with the cysteine (Cys-12) residue near the N-terminus at the active site of arsenate reductase and/or participates in catalysis (Rosen, 2002a Silver and Phung, 2005 Shi etal, 2003 Martin et al, 2001). 

A family of basic proteins associated with the chromatin in the nucleus of the cell. Protamines are characterized by a high content of arginine and replace histones in the process of spermiogenesis. See Lewis, S.D. and Ausid, J., Protamine-like proteins evidence for a novel chromatin structure, Biochem. Cell Biol. 80, 353-361,2002 Meistrich, M.L., Moha-patra, B., Shirley, C.R., and Zhao, M., Roles of transition nuclear proteins in spermiogenesis, Chromasoma 111, 483 88, 2003 Aoki,... 

Crane, B.R., A.S. Arvai, S. Ghosh, E.D. Getzoff, D.J. Stuehr, and J.A. Tainer (2000). Structures of the N-omega-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins. Biochem. 39, 4608-4621. 

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