Purification and characterization of recombinant malate synthase enzymes from Streptomyces coelicolor A3(2) and S. clavuligerus NRRL3585

2002 ◽  
Vol 28 (4) ◽  
pp. 239-243
Author(s):  
P Loke ◽  
L-L Goh ◽  
B Seng Soh ◽  
P Yeow ◽  
T-S Sim
Keyword(s):  
Streptomyces Coelicolor ◽  
Malate Synthase ◽  
Purification And Characterization

scholarly journals The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor

1990 ◽  
Vol 265 (3) ◽  
pp. 735-738 ◽  
Author(s):  
P J White ◽  
J Young ◽  
I S Hunter ◽  
H G Nimmo ◽  
J R Coggins
Keyword(s):  
Neurospora Crassa ◽  
Aspergillus Nidulans ◽  
Gel Electrophoresis ◽  
Streptomyces Coelicolor ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Kinetic Properties ◽  
Purification And Characterization ◽  
Large Oligomer

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.

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