The primary structure of omega-amino acid:pyruvate aminotransferase.

Properties of the bound coenzyme and subunit structure of omega-amino acid:pyruvate aminotransferase.

w-Amino acid:pyruvate aminotransferase of Pseudomonas sp. F-126 is composed of 1600 amino acids/ mol of enzyme, including 8 residues each of half-cystine and methionine/subunit. The enzyme was shown to consist of four subunits identical in molecular weight by sodium dodecyl sulfate-disc electrophoresis. The identity of the subunits is further suggested by determining NH2and COOH-terminal amino ...

Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum

The enzyme omega-transaminase catalyses the conversion of chiral omega-amines to ketones. The recombinant enzyme from Chromobacterium violaceum has been purified to homogeneity. The enzyme was crystallized from PEG 4000 using the microbatch method. Data were collected to 1.7 A resolution from a crystal belonging to the triclinic space group P1, with unit-cell parameters a = 58.9, b = 61.9, c = ...

Evaluation and impact of omega-3 supplementation with a period of selective aerobic exercise on liver enzymes (AST-ALT) of active student girls

Introduction: Liver enzymes are among clinical and biochemical parameters reflecting liver function in muscle exercises and Aspartate amino transferase (AST) and Alanine aminotransferase (ALT) enzymes are indicators of liver damage in sporting activities. However, AST and ALT liver enzymes are affected by supplementation with omega-3. In the present study, the effects of omega-3 supplementation...

-Amino Acid:Pyruvate Transaminase from Alcaligenes denitrificans Y2k-2: a New Catalyst for Kinetic Resolution of -Amino Acids and Amines

The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases.

The gene for thermostable D-amino acid aminotransferase from a thermophile, Bacillus species YM-1 was cloned and expressed efficiently in Escherichia coli. The entire covalent structure of the enzyme was determined from the nucleotide sequence of the cloned gene and mostly confirmed by amino acid sequences of tryptic peptides from the gene product. The polypeptide is composed of 282 amino acid ...