RT Journal Article
T1 Purification and properties of an unusual UDP-glucose dehydrogenase, NADPH-dependent, from Xanthomonas albilineans
A1 Blanch Rojo, María
A1 Legaz González, María Estrella
A1 Vicente Córdoba, Carlos
AB Xanthomonas albilineans produces a UDP-glucose dehydrogenase growing on sucrose. The enzyme oxidizes UDP-glucose to UDP-glucuronic acid by using molecular oxygen and NADPH. Kinetics of enzymatic oxydation of NADPH is linearly dependent on the amount of oxygen supplied. The enzyme has been purified at homogeneity. The value of pI of the purified enzyme is 8.98 and its molecular mass has been estimated as about 14 kDa. The enzyme shows a michaelian kinetics for UDP-glucose concentrations. The value of Km for UDP-glucose is 0.87 mM and 0.26 mM for NADPH, although the enzyme has three different sites to interact with NADPH. The enzyme is inhibited by UDP-glucose concentrations higher than 1.3 mM. N-Terminal sequence has been determined as IQPYNH.
PB Elsevier
SN 0944-5013
YR 2008
FD 2008
LK https://hdl.handle.net/20.500.14352/91744
UL https://hdl.handle.net/20.500.14352/91744
LA eng
NO Blanch, María, et al. «Purification and Properties of an Unusual UDP-Glucose Dehydrogenase, NADPH-Dependent, from Xanthomonas Albilineans». Microbiological Research, vol. 163, n.o 3, mayo de 2008, pp. 362-71.  https://doi.org/10.1016/j.micres.2006.07.011.
NO Ministerio de Ciencia y Tecnología (España)
DS Docta Complutense
RD 10 abr 2025