Molecular insights into the activity and mechanism of cyanide hydratase enzyme associated with cyanide biodegradation by Serratia marcescens

The present study provides molecular insights into the activity and mechanism of cyanide hydratase enzyme associated with degradation of cyanide compounds, using Serratia marcescens RL2b as a model organism. Resting cells harvested after 20 h achieved complete degradation of 12 mmol l − 1 cyanide in...

Full description

Saved in:
Bibliographic Details
Published in:Archives of microbiology 2018-08, Vol.200 (6), p.971-977
Main Authors: Kushwaha, Madhulika, Kumar, Virender, Mahajan, Rishi, Bhalla, Tek Chand, Chatterjee, Subhankar, Akhter, Yusuf
Format: Article
Language:English
Subjects:
Amino acids
Bacteria
Biochemistry
Biodegradation
Biomedical and Life Sciences
Biotechnology
Catalysis
Cell Biology
Cyanide hydratase
Cyanides
Ecology
Enzymes
High performance liquid chromatography
Life Sciences
Liquid chromatography
Microbial Ecology
Microbiology
Molecular chains
Nitrilase
Phylogeny
Proteins
Serratia marcescens
Short Communication
Structural analysis
Substrates
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The present study provides molecular insights into the activity and mechanism of cyanide hydratase enzyme associated with degradation of cyanide compounds, using Serratia marcescens RL2b as a model organism. Resting cells harvested after 20 h achieved complete degradation of 12 mmol l − 1 cyanide in approximately 10 h. High-performance liquid chromatography analysis of reaction samples revealed formation of formamide as the only end product, which confirmed the presence of cyanide hydratase activity in S. marcescens RL2b. Comparative structural analysis with the other nitrilase family proteins, which was carried out using a sequence of cyanide hydratase from a phylogenetically related strain S. marcescens WW4, also revealed subtle but significant differences in amino acid residues of the substrate-binding pocket and catalytic triad (Cys-Lys-Glu).
ISSN:0302-8933
1432-072X
DOI:10.1007/s00203-018-1524-0