PMID:6102910

Citation	Biellmann, JF, Eid, P, Hirth, C and Jörnvall, H (1980) Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Affinity labeling with the substrate analogue L-2-amino-4-oxo-5-chloropentanoic acid: an example of half-site reactivity. Eur. J. Biochem. 104:59-64
Abstract	The substrate binding site of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli was studied by affinity labeling with L-2-amino-4-oxo-5-chloropentanoic acid. The substrate analogue irreversibly inactivates the enzyme with pseudo-first-order kinetics and with a half-of-the-sites reactivity. The substrate aspartate beta-semialdehyde protects the enzyme against the inactivation. A single group is labeled at the active site and is concluded to be the side-chain of a histidine residue. The amino acid sequence around the active site residue was established from a peptic digest of the labeled enzyme: Phe-Val-Gly-Gly-Asp-(modified residue)-Thr-Val-Ser.
Links	PubMed
Keywords	Affinity Labels; Aspartate-Semialdehyde Dehydrogenase/metabolism; Binding Sites; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Kinetics; Levulinic Acids; Protein Binding
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