Plasma threonine

Table 1. Threonine requirement of 50W5 in early and late gestation based on indicator amino acid and plasma threonine concentration. 

Tyrosine phosphorylated IRS interacts with and activates PI 3-kinase [3]. Binding takes place via the SRC homology 2 (SH2) domain of the PI 3-kinase regulatory subunit. The resulting complex consisting of INSR, IRS, and PI 3-kinase facilitates interaction of the activated PI 3-kinase catalytic subunit with the phospholipid substrates in the plasma membrane. Generation of PI 3-phosphates in the plasma membrane reemits phospholipid dependent kinases (PDKl and PDK2) which subsequently phosphorylate and activate the serine/threonine kinase Akt (synonym protein... 

All isoforms of PKC are predominantly localized to the cytosol and, upon activation, undergo translocation to either plasma or nuclear membranes. However, newly synthesized PKCs are localized to the plasmalemma and are in an open conformation in which the auto inhibitory pseudosubstrate sequence is removed from the substrate binding domain. The maturation of PKC isoforms is effected by phosphoinositide-dependentkinase-I (PDK-I), which phosphorylates a conserved threonine residue in the activation loop of the catalytic (C4) domain [24]. This in turn permits the autophosphorylation of C-terminus threonine and serine residues in PKC, a step which is a prerequisite for catalytic activity (see also Chs 22 and 23). The phosphorylated enzyme is then released into the cytosol, where it is maintained in an inactive conformation by the bound pseudosubstrate. It was originally thought that 3-phosphoinositides such as PI(3,4)P2 and PI(3,4,5)P3 could directly activate PKCs. However, it now seems more likely that these lipids serve to activate PDK-1 (a frequent contaminant of PKC preparations). 

In some cases, the amino acid pattern on a paper chromatogram is very similar to that found in diseases of the renal tubules, such as cystinosis, where there is a failure to reabsorb all amino acids from the glomerular filtrate and, in consequence, the urinary amino acid pattern resembles that of plasma (W6, W9). In other cases the aminoaciduria is less marked and the amino acids found in greatest excess are glycine, alanine, serine, threonine, and glutamine. In some cases no aminoaciduria has been detected. 

A T-C polymorphism was described in the sequence of apo(a)-KIV10 (V6), corresponding to nucleotide 12,605 of the published cDNA sequence (M24). This variant results in the substitution of a methionine (ATG) with a threonine (ACG) at this position. No correlation was observed between the polymorphism and plasma Lp(a) levels. Although the Met-Thr substitution is present within the lysine binding pocket in KIV10, its effect on lysine binding properties of this kringle remains to be determined. 

Lecchi, S. Allen, K. E. Pardo, J. P Mason, A. B. Slayman, C. W. Conformational Changes of Yeast Plasma Membrane H+-ATPase during Activation by Glucose Role of Threonine-912 in the Carboxy-Terminal Tail. Biochemistry 2003, 44, 16624-16632. 

Amino groups are tunneled to glutamate from all amino acids except lysine and threonine. The enzymes are aminotransferases, and they are reversible. The two most important of these enzymes are alanine aminotransferase (ALT) and aspartate aminotransferase (AST). Aminotransferases require pyridoxal phosphate as a coenzyme. The presence of elevated levels of aminotransferases in the plasma can be used to diagnose liver disease. 

H-ras Harvey murine sarcoma p21V-Hlus p21c H-ras Threonine kinase Plasma membrane... 

Human plasma Cardiovascular 864 status in healthy voluntaries NMR 3-Hydroxybutyrate a-Ketoglutarate Threonine Dimethylglycine (19)... 

---