Literature DB >> 27566691

Arylmalonate decarboxylase-a highly selective bacterial biocatalyst with unknown function.

Kenji Miyamoto1, Robert Kourist2.   

Abstract

Bacterial arylmalonate decarboxylase (AMDase) shows high enantioselectivity and a broad substrate spectrum in the asymmetric synthesis of optically pure arylaliphatic carboxylic acids. The determination of the structure of AMDase has greatly extended the understanding of the catalytic mechanism of this unique cofactor-free decarboxylase and allowed the generation of tailor-made enzyme variants with improved catalytic properties. Despite this increase in knowledge and applicability, the natural role of the enzyme remains unknown. This mini-review summarizes the recent findings on the molecular mechanism and the synthetic application of the enzyme.

Entities:  

Keywords:  Asymmetric synthesis; Biocatalysis; Catalytic promiscuity; Cofactor-free decarboxylases; Enzyme engineering; Lyases

Mesh:

Substances:

Year:  2016        PMID: 27566691     DOI: 10.1007/s00253-016-7778-z

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


  2 in total

1.  Ground-State Destabilization by Active-Site Hydrophobicity Controls the Selectivity of a Cofactor-Free Decarboxylase.

Authors:  Michal Biler; Rory M Crean; Anna K Schweiger; Robert Kourist; Shina Caroline Lynn Kamerlin
Journal:  J Am Chem Soc       Date:  2020-11-12       Impact factor: 15.419

2.  Editorial: Applied Microbiology for Chemical Syntheses.

Authors:  Robert Kourist; Javier González-Sabín; Bettina Siebers; Mattijs Julsing
Journal:  Front Microbiol       Date:  2017-10-11       Impact factor: 5.640

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.