Properties of the enzyme expressed by the Pseudomonas saccharophila maltotetraohydrolase gene (mta) in Escherichia coli.
The maltotetraohydrolase gene (mta) from Pseudomonas saccharophila was expressed in Escherichia coli JM109. Maltotetraohydrolase was produced mostly (approximately 90%) in the periplasmic space. The amino-terminal amino acid sequence and molecular weight of the recombinant enzyme were identical with those of the native enzyme, and there was no significant difference in the substrate specificity and modes of action. This system for maltotetraohydrolase expression is useful for studies of the structure and function of the enzyme.
Zhou
J H
JH
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Baba
T
T
Takano
T
T
Kobayashi
S
S
Arai
Y
Y
D015153:Blotting, Western; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D007700:Kinetics; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013816:Thermodynamics; D000520:alpha-Glucosidases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D011994:Recombinant Proteins; D000520:alpha-Glucosidases; C020135:glucan 1,4-maltotetraohydrolase