The cold-active M1 aminopeptidase from the Arctic bacterium Colwellia psychrerythraea

Bauvois, Cédric; Huston, Adrienne L.; Feller, Georges

doi:10.1016/B978-0-443-28849-4.00023-0

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The cold-active M1 aminopeptidase from the Arctic bacterium Colwellia psychrerythraea

Bauvois, Cédric; Huston, Adrienne L.; Feller, Georges

2025 • In Handbook of Proteolytic Enzymes: Metallopeptidases

Peer reviewed

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https://hdl.handle.net/2268/348083

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10.1016/B978-0-443-28849-4.00023-0

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Keywords :

biophysics; cold-active proteases; Colwellia psychrerythraea; crystal structure; differential scanning calorimetry; epoxide hydrolase; M1 aminopeptidases; psychrophiles; zinc metalloproteases; zinc-binding site; Amino peptidase; Cold-active protease; Crystals structures; Epoxide hydrolases; M1 aminopeptidase; Psychrophile; Scanning calorimetry; Zinc metalloprotease; Zinc-binding sites; Biochemistry, Genetics and Molecular Biology (all)

Abstract :

[en] The subject of this chapter is the cold-active M1 aminopeptidase from the Arctic bacterium Colwellia psychrerythraea. This enzyme has a preference for leucyl bonds and is most active at a temperature of −1°C. The sequence and structure are known, and the aminopeptidase is a Glu-zincin most closely related to leukotriene A4 hydrolase.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Bauvois, Cédric; LABIRIS, Brussels, Belgium

Huston, Adrienne L.; Verenium Corporation, San Diego, United States

Feller, Georges ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques

Language :

English

Title :

The cold-active M1 aminopeptidase from the Arctic bacterium Colwellia psychrerythraea

Publication date :

2025

Main work title :

Handbook of Proteolytic Enzymes: Metallopeptidases

Publisher :

Elsevier

ISBN/EAN :

978-0-443-28849-4
978-0-443-28850-0

Peer reviewed :

Peer reviewed

Additional URL :

https://api.elsevier.com/content/article/PII:B9780443288494000230?httpAccept=text/xml

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since 23 August 2026

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Bibliography

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