Isolation and characterization of a novel 5-oxoprolinase (without ATP-hydrolyzing) from Alcaligenes faecalis N-38A.
A screening test was undertaken to isolate a microorganism that produced 5-oxoprolinase (without ATP-hydrolyzing). The 5-oxoprolinase (without ATP-hydrolyzing) activity (decyclization activity toward L-pyroglutamate) was found in a cell-free extract of Alcaligenes faecalis N-38A, newly isolated from a soil sample. The enzyme was purified as a homogeneous preparation. The molecular weight of the enzyme was estimated to be 47,000. The decyclization activity was specific for L-pyroglutamate, and independent of ATP and metal ions. The reaction was a reversible one, i.e., cyclization reaction of L-glutamate to yield pyroglutamate was identified.
Murao
S
S
Department of Applied Microbial Technology, Kumamoto Institute of Technology, Japan.
Nishimura
A
A
Ozaki
Y
Y
Oyama
H
H
Shin
T
T
D000421:Alcaligenes / Q000201:enzymology*; D018698:Glutamic Acid / Q000378:metabolism; D011761:Pyrrolidonecarboxylic Acid / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D018698:Glutamic Acid; D011761:Pyrrolidonecarboxylic Acid