Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/1615
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Type: Journal article
Title: The characterization of a (nutritionally important) proline iminopeptidase from Eikenella corrodens
Author: Gully, N.
Rogers, A.
Citation: Molecular Oral Microbiology, 2001; 16(6):370-375
Publisher: Munksgaard Int Publ Ltd
Issue Date: 2001
ISSN: 0902-0055
1399-302X
Statement of
Responsibility: 
N. J. Gully, A. H. Rogers
Abstract: Eikenella corrodens generates energy primarily through the oxidative deamination of specific amino acids, a process that is coupled to dissimilatory nitrate reduction to nitrite. Cell yields resulting from chemostat-growth of the organism in simple, chemically defined media containing varying amounts of proline confirm that this amino acid is a likely source of energy for E. corrodens in the oral environment. The importance of proline in ATP generation by the organism is reflected in molar growth yields, which showed that biomass production per mole of this amino acid was significantly higher than that for other amino acids. The organism was found to express, constitutively, the enzyme proline iminopeptidase, which releases proline from the N-terminus of small peptides. The enzyme was partially purified and characterized and found to exist in the cytoplasm as a 35 kDa monomer. Inhibition studies showed that the enzyme, although classified as a serine protease, also appears to require thiol groups for activity, a finding which is consistent with previous reports. The enzyme obeyed Michaelis-Menten kinetics and was found to have a Km value of 0.223 mM for the substrate proline-p-nitroanilide.
Keywords: Eikenella corrodens
proline iminopeptidase
nutrition
Description: The definitive version is available at www.blackwell-synergy.com
DOI: 10.1034/j.1399-302X.2001.160609.x
Appears in Collections:Aurora harvest 2
Dentistry publications

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