Enzymatic Analysis of Reconstituted Archaeal Exosomes

2019 ◽  
pp. 63-79
Author(s):  
Elena Evguenieva-Hackenberg ◽  
A. Susann Gauernack ◽  
Linlin Hou ◽  
Gabriele Klug
Keyword(s):  
Enzymatic Analysis

Deciphering characteristics of the designer cellulosome from Bacillus subtilis WB800N via enzymatic analysis

2017 ◽  
Vol 117 ◽  
pp. 147-155 ◽  
Author(s):  
Chia-Chi Lin ◽  
Cally Joe San Yap ◽  
Shu-Chen Kan ◽  
Nai-Chi Hsueh ◽  
Liang-Yu Yang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Enzymatic Analysis ◽  
Bacillus Subtilis Wb800n ◽  
Designer Cellulosome

scholarly journals Enzymatic analysis of cyanogenic glycosides. II. A simple method by using a microdiffusional apparatus.

1988 ◽  
Vol 36 (1) ◽  
pp. 249-253
Author(s):  
TOMOKO NASHIDA(nee ITOH) ◽  
TAKAYUKI SHIRAISHI ◽  
YUTAKA UDA
Keyword(s):  
Cyanogenic Glycosides ◽  
Enzymatic Analysis ◽  
Simple Method

scholarly journals Identification and Characterization of a New Enoyl Coenzyme A Hydratase Involved in Biosynthesis of Medium-Chain-Length Polyhydroxyalkanoates in Recombinant Escherichia coli

2003 ◽  
Vol 185 (18) ◽  
pp. 5391-5397 ◽  
Author(s):  
Si Jae Park ◽  
Sang Yup Lee
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Chain Length ◽  
Biosynthetic Pathway ◽  
Pha Synthase ◽  
Enzymatic Analysis ◽  
E Coli ◽  
Medium Chain ◽  
Medium Chain Length ◽  
Enoyl Coa Hydratase

ABSTRACT The biosynthetic pathway of medium-chain-length (MCL) polyhydroxyalkanoates (PHAs) from fatty acids has been established in fadB mutant Escherichia coli strain by expressing the MCL-PHA synthase gene. However, the enzymes that are responsible for the generation of (R)-3-hydroxyacyl coenzyme A (R3HA-CoAs), the substrates for PHA synthase, have not been thoroughly elucidated. Escherichia coli MaoC, which is homologous to Pseudomonas aeruginosa (R)-specific enoyl-CoA hydratase (PhaJ1), was identified and found to be important for PHA biosynthesis in a fadB mutant E. coli strain. When the MCL-PHA synthase gene was introduced, the fadB maoC double-mutant E. coli WB108, which is a derivative of E. coli W3110, accumulated 43% less amount of MCL-PHA from fatty acid compared with the fadB mutant E. coli WB101. The PHA biosynthetic capacity could be restored by plasmid-based expression of the maoCEc gene in E. coli WB108. Also, E. coli W3110 possessing fully functional β-oxidation pathway could produce MCL-PHA from fatty acid by the coexpression of the maoCEc gene and the MCL-PHA synthase gene. For the enzymatic analysis, MaoC fused with His6-Tag at its C-terminal was expressed in E. coli and purified. Enzymatic analysis of tagged MaoC showed that MaoC has enoyl-CoA hydratase activity toward crotonyl-CoA. These results suggest that MaoC is a new enoyl-CoA hydratase involved in supplying (R)-3-hydroxyacyl-CoA from the β-oxidation pathway to PHA biosynthetic pathway in the fadB mutant E. coli strain.

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