The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor.
The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor. The subunit Mr estimated from polyacrylamide-gel electrophoresis in the presence of SDS was 16,000. The native Mr estimated by gel filtration on a Superose 6 column was 209,000, indicating that the enzyme is a large oligomer. The enzyme was found to be extremely thermostable. This stability, along with the structural and kinetic properties of the enzyme, suggest that it is very similar to the quinate-inducible 3-dehydroquinase found in Neurospora crassa and Aspergillus nidulans. This similarity was confirmed by direct N-terminal sequencing.
White
P J
PJ
Department of Biochemistry, University of Glasgow, U.K.
Young
J
J
Hunter
I S
IS
Nimmo
H G
HG
Coggins
J R
JR
D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006836:Hydro-Lyases / Q000032:analysis / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D013302:Streptomyces / Q000201:enzymology*; D014578:Uroporphyrins / Q000096:biosynthesis
D014578:Uroporphyrins; C014188:sirohydrochlorin; D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase