Purification and characterization of N‐acyl‐D‐glutamate deacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A‐6
Open Access
- 2 September 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 289 (1) , 44-46
- https://doi.org/10.1016/0014-5793(91)80904-h
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 K ms for N‐acetyl, N‐butyryl and N‐propionyl derivatives of D‐glutamate were 0.129, 0.066 and 0.01 mM, respectively.Keywords
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