1mgv | pdb_00001mgv

Crystal Structure of the R391A Mutant of 7,8-Diaminopelargonic Acid Synthase

spinqualitylabelsall models 1mgv, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mgv is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IPA, NA, PLP Related: 1qj5, 1dty, 1qj3 Gene: bioA ("Bacillus coli" Migula 1895) Activity: Adenosylmethionine--8-amino-7-oxononanoate transaminase, with EC number 2.6.1.62 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [BIOA_ECOLI] Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. 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 PubMed 7,8-diaminopelargonic acid (DAPA) synthase (EC 2.6.1.62) is a pyridoxal phosphate (PLP)-dependent transaminase that catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form DAPA in the antepenultimate step in the biosynthesis of biotin. The wild-type enzyme has a steady-state kcat value of 0.013 s(-1), and the K(m) values for SAM and KAPA are 150 and <2 microM, respectively. The k(max) and apparent K(m) values for the half-reaction of the PLP form of the enzyme with SAM are 0.016 s(-1) and 300 microM, respectively, while those for the reaction with DAPA are 0.79 s(-1) and 1 microM. The R391A mutant enzyme exhibits near wild-type kinetic parameters in the reaction with SAM, while the apparent K(m) for DAPA is increased 180-fold. The 2.1 A crystal structure of the R391A mutant enzyme shows that the mutation does not significantly alter the structure. These results indicate that the conserved arginine residue is not required for binding the alpha-amino acid SAM, but it is important for recognition of DAPA. The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation.,Eliot AC, Sandmark J, Schneider G, Kirsch JF Biochemistry. 2002 Oct 22;41(42):12582-9. PMID:12379100 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 7%2C8-diaminopelargonic acid synthetase

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