Crystallization of Arthrobacter sp. strain 1C N-(1-D-carboxyethyl)-L- norvaline dehydrogenase and its complex with NAD+.
The novel NAD+-linked opine dehydrogenase from a soil isolate Arthrobacter sp. strain 1C belongs to an enzyme superfamily whose members exhibit quite diverse substrate specificities. Crystals of this opine dehydrogenase, obtained in the presence or absence of co-factor and substrates, have been shown to diffract to beyond 1.8 A resolution. X-ray precession photographs have established that the crystals belong to space group P21212, with cell parameters a = 104.9, b = 80.0, c = 45.5 A and a single subunit in the asymmetric unit. The elucidation of the three-dimensional structure of this enzyme will provide a structural framework for this novel class of dehydrogenases to enable a comparison to be made with other enzyme families and also as the basis for mutagenesis experiments directed towards the production of natural and synthetic opine-type compounds containing two chiral centres.
Britton
K L
KL
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, England. k.britton@sheffield.ac.uk
Rogers
H F
HF
Asano
Y
Y
Dairi
T
T
Kato
Y
Y
Stillman
T J
TJ
D001173:Arthrobacter / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D009243:NAD / Q000737:chemistry*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry*
D009243:NAD; D000587:Oxidoreductases Acting on CH-NH Group Donors; C113417:N-(1-D-carboxyethyl)-L-norvaline dehydrogenase