TY - JOUR
T1 - Purification and characterization of N-acyl-D-glutamate deacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6.
AU - Sakai, Kenji
AU - Imamura, Kazuyuki
AU - Sonoda, Yuji
AU - Kido, Hiroyuki
AU - Moriguchi, Mitsuaki
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1991/9/2
Y1 - 1991/9/2
N2 - The purification and properties of N-acyl-D-glutamate deacylase from the cell extracts of Alcaligenes xylosoxydans subsp. xylosoxydans A-6 were studied. The two active fractions (peaks I and II) were obtained by a Mono Q column chromatography. The predominant enzyme (peak I) has been purified, 1960-fold to homogeneity and characterized. The enzyme was a monomer with a molecular weight of 59 000. The optimum pH and the isoelectric point were 8.0 and 5.5, respectively. The enzyme catalyzed the hydrolysis of N-acyl derivatives of D-glutamate. The Kms for N-acetyl, N-butyryl and N-propionyl derivatives of D-glutamate were 0.129, 0.066 and 0.01 mM, respectively.
AB - The purification and properties of N-acyl-D-glutamate deacylase from the cell extracts of Alcaligenes xylosoxydans subsp. xylosoxydans A-6 were studied. The two active fractions (peaks I and II) were obtained by a Mono Q column chromatography. The predominant enzyme (peak I) has been purified, 1960-fold to homogeneity and characterized. The enzyme was a monomer with a molecular weight of 59 000. The optimum pH and the isoelectric point were 8.0 and 5.5, respectively. The enzyme catalyzed the hydrolysis of N-acyl derivatives of D-glutamate. The Kms for N-acetyl, N-butyryl and N-propionyl derivatives of D-glutamate were 0.129, 0.066 and 0.01 mM, respectively.
UR - http://www.scopus.com/inward/record.url?scp=0025768002&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025768002&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(91)80904-H
DO - 10.1016/0014-5793(91)80904-H
M3 - Article
C2 - 1894006
AN - SCOPUS:0025768002
VL - 289
SP - 44
EP - 46
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -