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Lysine biochemical structure

Kochhar, S. Kochhar, V.K. Sane, P.V. Subunit structure of lysine sensitive aspartate kinase from spinach leaves. Biochem. Mol. Biol. Int., 44, 795-806 (1998)... [Pg.331]

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. ... [Pg.1856]

The puzzle of how one ion channel could be activated by such a broad range of irritants (e.g., AITC, formalin, alUcin, diaUyl disulfide, acrolein, cinnamaldehyde) with minimal structural similarity was reconciled by the discovery that TRPAl is activated when electrophiles form covalent adducts with three cysteines (and, in human TRPAl, one lysine) within the channel s cytosolic N terminus (Hinman et al. 2006 Macpherson et al. 2007a). This suggests that any cysteine-reactive electrophile that can access these crucial residues has the potential to activate TRPAl and evoke nociceptive reflexes. In support of this, iodoacetamide, the cysteine-reactive tool molecule often used in biochemical experiments, activates TRPAl (albeit with very low potency) and evokes nocifensive behaviors in wild-type but not TRPAl knockout mice (Macpherson et al. 2007b). [Pg.135]

Kato C, Kurihara T, Kobashi N, Yamane H, Nishiyama M (2004) Conversion of feedback regulation in aspartate kinase by domain exchange. Biochem Bioph Res Co 316 802-808 Kim YH, Park JS, Cho JY, Cho KM, Park YH, Lee J (2004) Proteomic response analysis of a threonine-overproducing mutant of Escherichia coli. Biochem J 381 823-829 Klaffl S, Eikmanns BJ (2010) Genetic and functional analysis of the soluble oxaloacetate decarboxylase from Corynebacterium glutamicum. J Bacterid 192 2604-2612 Komatsubara S, Kisumi M, Murata K, Chibata 1 (1978) Threonine production by regulatory mutants of Serratia marcescens. Appl Environ Microbiol 35 834-840 Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK (2006) Structures of R- and T-state Escherichia coli aspartokinase 111 mechanisms of the allosteric transition and inhibition by lysine. J Biol Chem 281 31544-31552... [Pg.300]


See other pages where Lysine biochemical structure is mentioned: [Pg.594]    [Pg.150]    [Pg.35]    [Pg.176]    [Pg.182]    [Pg.347]    [Pg.9]    [Pg.29]    [Pg.29]    [Pg.57]    [Pg.163]    [Pg.31]    [Pg.375]    [Pg.264]    [Pg.140]    [Pg.272]    [Pg.310]    [Pg.594]    [Pg.176]    [Pg.110]    [Pg.202]    [Pg.241]    [Pg.279]    [Pg.299]    [Pg.311]    [Pg.344]    [Pg.154]    [Pg.135]    [Pg.400]    [Pg.214]    [Pg.22]    [Pg.388]    [Pg.617]    [Pg.1195]    [Pg.1303]    [Pg.650]    [Pg.227]    [Pg.10]    [Pg.143]    [Pg.24]    [Pg.90]    [Pg.218]    [Pg.152]    [Pg.2119]    [Pg.3429]    [Pg.301]    [Pg.114]   
See also in sourсe #XX -- [ Pg.343 ]




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Biochemical structures

Lysine structure

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