Structural highlights
Function[OAPT_PSEPU] Catalyzes transamination between a variety of omega-amino acids, mono and diamines, and pyruvate. Plays a pivotal role in the metabolism of the omega amino acids.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structure of omega-amino acid:pyruvate aminotransferase from Pseudomonas sp. F-126, an isologous alpha 4 tetramer containing pyridoxal 5'-phosphate (PLP) as a cofactor, has been determined at 2.0 A resolution. The diffraction data were collected with a newly developed Weissenberg camera with a Fuji Imaging Plate, using synchrotron radiation. The mean figure-of-merit was 0.57. The subunit is rich in secondary structure and comprises two domains. PLP is located in the large domain. The high homology in the secondary structure between this enzyme and aspartate aminotransferase strongly indicates that these two types of enzymes have evolved from a common ancestor. Crystal structure analysis of omega-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation.,Watanabe N, Sakabe K, Sakabe N, Higashi T, Sasaki K, Aibara S, Morita Y, Yonaha K, Toyama S, Fukutani H J Biochem. 1989 Jan;105(1):1-3. PMID:2500426[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 22:58, 5 August 2016.