N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2
Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue.
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), PROTEIN SEQUENCE OF 1-9, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism.
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH NADP.
The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP ANALOG, MUTAGENESIS OF ASN-98; LYS-176 AND GLU-256.
pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NADP, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-72 AND SER-244.
Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity.
According to the literature [6], this enzyme catalyzes the following reaction: (0) The sidechain of Glu256 and the amide groups of both sidechain and mainchain of Asn98 may modulate the activity of nicotinamide group through ribose hydroxyl groups. Moreover, the sidechain of Asn98 might modulate the activity of Lys176 as well as the substrate through its carboxyl group. (1) The pro-S hydride of NADPH transfers to the si-face of substrate, 2-dehydropantoate (or ketopantoate). At the same time, Lys176 acts as a general acid to protonate the C2 carbonyl oxygen during the developing C2-alkoxide.