Literature DB >> 17318535

Bacterial beta-peptidyl aminopeptidases: on the hydrolytic degradation of beta-peptides.

B Geueke1, H-P E Kohler.   

Abstract

The special chemical and biological features of beta-peptides have been investigated intensively during recent years. Many studies emphasize the restricted biodegradability and the high metabolic stability of this class of compounds. beta-Peptidyl aminopeptidases form the first family of enzymes that hydrolyze a variety of short beta-peptides and beta-amino-acid-containing peptides. All representatives of this family were isolated from Gram-negative bacteria. The substrate specificities of the peptidases vary greatly, but the enzymes have common structural properties, and a similar reaction mechanism can be expected. This review gives an overview on the beta-peptidyl aminopeptidases with emphasis on their biochemical and structural properties. Their possible physiological function is discussed. Functionally and structurally related enzymes are compared to the beta-peptidyl aminopeptidases.

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Year:  2007        PMID: 17318535     DOI: 10.1007/s00253-007-0872-5

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   4.813


  5 in total

1.  β-Aminopeptidases: Insight into Enzymes without a Known Natural Substrate.

Authors:  Marietta John-White; James Gardiner; Priscilla Johanesen; Dena Lyras; Geoffrey Dumsday
Journal:  Appl Environ Microbiol       Date:  2019-07-18       Impact factor: 4.792

2.  Crystal structure of a β-aminopeptidase from an Australian Burkholderia sp.

Authors:  Marietta John-White; Geoff J Dumsday; Priscilla Johanesen; Dena Lyras; Nyssa Drinkwater; Sheena McGowan
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2017-06-17       Impact factor: 1.056

3.  Characterization of a new L-carnosine synthase mined from deep-sea sediment metagenome.

Authors:  Jiajia She; Lihong Fu; Xiaowei Zheng; Jing Li; Limin Wang; Bo Yu; Jiansong Ju
Journal:  Microb Cell Fact       Date:  2022-06-27       Impact factor: 6.352

4.  Biochemical properties and crystal structure of a β-phenylalanine aminotransferase from Variovorax paradoxus.

Authors:  Ciprian G Crismaru; Gjalt G Wybenga; Wiktor Szymanski; Hein J Wijma; Bian Wu; Sebastian Bartsch; Stefaan de Wildeman; Gerrit J Poelarends; Ben L Feringa; Bauke W Dijkstra; Dick B Janssen
Journal:  Appl Environ Microbiol       Date:  2012-10-19       Impact factor: 4.792

5.  Substrate stereoselectivity of poly(Asp) hydrolase-1 capable of cleaving β-amide bonds as revealed by investigation of enzymatic hydrolysis of stereoisomeric β-tri(Asp)s.

Authors:  Tomohiro Hiraishi; Hideki Abe; Mizuo Maeda
Journal:  AMB Express       Date:  2015-06-04       Impact factor: 3.298

  5 in total

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