Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1991 Sep 2;289(1):44-6.
doi: 10.1016/0014-5793(91)80904-h.

Purification and Characterization of N-acyl-D-glutamate Deacylase From Alcaligenes Xylosoxydans Subsp. Xylosoxydans A-6

Affiliations
Free article

Purification and Characterization of N-acyl-D-glutamate Deacylase From Alcaligenes Xylosoxydans Subsp. Xylosoxydans A-6

K Sakai et al. FEBS Lett. .
Free article

Abstract

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.

Similar articles

See all similar articles

Cited by 2 articles

LinkOut - more resources

Feedback