PMID:1463470
| Citation |
Laber, B, Gomis-Rüth, FX, Romão, MJ and Huber, R (1992) Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization. Biochem. J. 288 ( Pt 2):691-5 |
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| Abstract |
Escherichia coli dihydrodipicolinate synthase (DHDPS) (EC 4.2.1.52), the first enzyme unique to lysine biosynthesis, catalyses the condensation of pyruvate and aspartate beta-semialdehyde (ASA) by a ping-pong mechanism. Pyruvate binds first to the enzyme, forming a Schiff base with the epsilon-amino group of Lys-161, followed by binding of ASA. Km values of 0.57 and 0.55 mM were determined for pyruvate and DL-ASA respectively. 3-Bromopyruvate inhibits DHDPS with a Ki of 1.6 mM. DHDPS is 50% inhibited by 1.0 mM-L-lysine, 1.2 mM-sodium dipicolinate or 4.6 mM-S-2-aminoethyl-L-cysteine. Crystals of DHDPS diffracting to beyond a resolution of 0.24 nm (2.4 A) were obtained under several experimental conditions. Diffraction patterns were compatible with trigonal space groups P3(1)21 or P3(2)21, with unit-cell parameters a = b = 12.26 nm and c = 11.19 nm. The density of the crystals indicates the presence of a dimer of DHDPS subunits per asymmetric unit. |
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| Keywords |
Amino Acid Sequence; Binding Sites; Chromatography; Crystallography; Escherichia coli/enzymology; Hydro-Lyases/antagonists & inhibitors; Hydro-Lyases/chemistry; Hydro-Lyases/isolation & purification; Hydro-Lyases/ultrastructure; Kinetics; Molecular Sequence Data; Molecular Weight; Peptide Fragments/chemistry; Sequence Alignment; X-Ray Diffraction |
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