Disease relevance of Acetylalanine

• A surface antigen consisting of aminoglucuronic acid and N-acetyl-L-alanine was isolated from the culture filtrates of two human strains of Staphylococcus aureus [1].
• Cell cycle phases of two human lung tumor cell lines derived from squamous cell carcinoma and pulmonary metastasis of a rhabdomyosarcoma (HS 24 and HS 57) and N-acetylalanine aminopeptidase activity [2].
• The catalytic concentration of N-acetylalanine aminopeptidase was determined in erythrocytes, polymorphonuclear leukocytes, lymphocytes, alveolar macrophages, human lung fibroblasts, human lung cancer cells, human umbilical vein endothelial cells, mice Leydig cells, rat tumour cells, and endothelial cells from hog and bovine lung [3].

High impact information on Acetylalanine

• Acetylalanine chloromethyl ketone inactivated the enzyme following pseudo-first order kinetics; and Ac-Ala, a competitive inhibitor, protected the enzyme from this inactivation [4].
• Reduced glutathione and L-cysteine also blocked Smad2 and TIMP-3 induction by TGF-beta1, whereas a nonthiol, N-acetylalanine, did not [5].
• One of these proteases is characterized by its preference for N-acetyl-L-alanine-alpha-naphthylester as substrate and by its genetic linkage to bt, a coat color marker of chromosome 15 [6].
• N-Formyl-L-alanine and N-acetyl-L-alanine are also hydrolyzed by the enzyme, but the rate of hydrolysis is lower than the rate for N-carbamoyl-L-alanine [7].
• Bovine brain heparin-binding growth factor 1 (HBGF-1), a single polypeptide (Mr 17,400) with an amino-terminal acetylalanine and three cysteines within the sequence, isolates in multiple truncated and chromatographic forms [8].

Biological context of Acetylalanine

• However, the cell cycle phase of N-acetylalanine aminopeptidase synthesis could not be determined [2].
• Monoclonal antibodies have been elicited against an achiral rhodium complex and this complex was used in the presence of a resultant antibody, 1G8, for the catalytic hydrogenation of 2-acetamidoacrylic acid to produce N-acetyl-l-alanine in high (>98%) enantiomeric excess [9].

Anatomical context of Acetylalanine

• N-Acetylalanine aminopeptidase, a new enzyme from human erythrocytes [10].

Associations of Acetylalanine with other chemical compounds

• Pyruvic acid and ammonia reacted to give N-acetylalanine, which formed alanine in a 3-7% overall yield upon hydrolysis [11].
• The hydrolytic activity of the enzyme toward N-acetyl-L-alanine p-nitroanilide at the optimum pH value was increased twofold in the presence of the chloride anion [12].
• The active agents in the neural tissue extract are heparin-binding polypeptides (prostatropins), the predominant form of which has a molecular weight of 17400 and an acetylalanine at the aminoterminus [13].
• Following the treatment with an acylamino-acid releasing enzyme, the blocked NH2-terminal amino acid was identified to be acetylalanine [14].

Gene context of Acetylalanine

• From sequence analysis of the cDNA and the N- and C-terminal amino acid analyses of the purified protein, it is deduced that porcine kidney ACY-1 consists of two identical subunits (M(r) 45,260), each of which consists of a single chain of 406 amino acids with acetylalanine at the N-terminus [15].
• OPH showed ACPH activity when N-acetyl-L-alanine p-nitroanilide and N-acetylmethionyl L-alanine were used as substrates [16].
• The blocked amino terminus of cytochrome b5 was identified as N-acetylalanine [17].
• The blocked amino-terminal residue of rat liver serine dehydratase was shown to be acetylalanine by analysis of an isolated amino-terminal peptide after digestion with acylamino acid-releasing enzyme [18].

References