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Enzymatic breakdown of poly-?-D-glutamic acid in Bacillus licheniformis: Identification of a polyglutamyl ?-hydrolase enzyme

Enzymatic breakdown of poly-?-D-glutamic acid in Bacillus licheniformis: Identification of a polyglutamyl ?-hydrolase enzyme
Enzymatic breakdown of poly-?-D-glutamic acid in Bacillus licheniformis: Identification of a polyglutamyl ?-hydrolase enzyme
A polyglutamyl gamma -hydrolase enzyme has been identified which catalyses the hydrolytic breakdown of poly-gamma -D-glutamic acid (PGA) from Bacillus licheniformis 9945a. The enzyme was found to be physically associated with the polymer and was activated by Zn2+ or Ca2+ salts. The enzyme can be solubilized from the polymer by treatment with 0.5% SDS and 1 mM ZnCl2 and can then be renatured onto exogenous PGA upon dilution below the detergent critical micellar concentration. The enzyme was partially purified by affinity chromatography, using immobilized PGA. Peptide thioesters containing one and two gamma -glutamyl units were synthesized as potential chromogenic substrates but showed no activity with the solubilized enzyme. Examination of C-14-labeled reaction products indicated that the enzyme is an endo-type hydrolase.
escherichia-coli k-12, poly(gamma-d-glutamyl) capsule, transpeptidase, purification, biosynthesis, metabolism, chemistry, gene
1525-7797
75-83
King, Elizabeth C.
ca115d1e-04b1-433a-b677-24ac944bb764
Blacker, A. John
d81f04fe-40a0-4d93-9ec3-2387f25adc69
Bugg, Timothy D.H.
97fe3334-49aa-4a52-a181-602fd7780d8b
King, Elizabeth C.
ca115d1e-04b1-433a-b677-24ac944bb764
Blacker, A. John
d81f04fe-40a0-4d93-9ec3-2387f25adc69
Bugg, Timothy D.H.
97fe3334-49aa-4a52-a181-602fd7780d8b

King, Elizabeth C., Blacker, A. John and Bugg, Timothy D.H. (2000) Enzymatic breakdown of poly-?-D-glutamic acid in Bacillus licheniformis: Identification of a polyglutamyl ?-hydrolase enzyme. Biomacromolecules, 1 (1), 75-83. (doi:10.1021/bm990001n). (PMID:11709846)

Record type: Article

Abstract

A polyglutamyl gamma -hydrolase enzyme has been identified which catalyses the hydrolytic breakdown of poly-gamma -D-glutamic acid (PGA) from Bacillus licheniformis 9945a. The enzyme was found to be physically associated with the polymer and was activated by Zn2+ or Ca2+ salts. The enzyme can be solubilized from the polymer by treatment with 0.5% SDS and 1 mM ZnCl2 and can then be renatured onto exogenous PGA upon dilution below the detergent critical micellar concentration. The enzyme was partially purified by affinity chromatography, using immobilized PGA. Peptide thioesters containing one and two gamma -glutamyl units were synthesized as potential chromogenic substrates but showed no activity with the solubilized enzyme. Examination of C-14-labeled reaction products indicated that the enzyme is an endo-type hydrolase.

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More information

Published date: 4 February 2000
Keywords: escherichia-coli k-12, poly(gamma-d-glutamyl) capsule, transpeptidase, purification, biosynthesis, metabolism, chemistry, gene

Identifiers

Local EPrints ID: 19027
URI: http://eprints.soton.ac.uk/id/eprint/19027
ISSN: 1525-7797
PURE UUID: c2a679a5-c989-419f-a69c-538aea9110df

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Date deposited: 18 Jan 2006
Last modified: 15 Jul 2019 19:27

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