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Physical and kinetic effects on induction of various linker regions in beta-galactosidase/galactose dehydrogenase fusion enzymes

Ljung, Sarah; Bülow, L LU and Carlsson, Hélen (1996) In Biochimica et Biophysica Acta 1293(1). p.60-154
Abstract

To examine the role of the connecting region in the artificial bifunctional enzyme beta-galactosidase/galactose dehydrogenase, linkers of different length were inserted between the catalytic units. The specific activity of the galactose dehydrogenase part of the complex was increased when longer linkers (9 and 13 amino acids) were used as connectors. These bifunctional enzymes were predominantly found to comprise hexamers, however, complexes of higher molecular weight were also formed. The sequential reaction was carried out more efficiently when hybrid enzymes with the longer linkers were used as demonstrated both in vitro by using purified protein preparations as well as in vivo by determining the growth rates of recombinant E. coli... (More)

To examine the role of the connecting region in the artificial bifunctional enzyme beta-galactosidase/galactose dehydrogenase, linkers of different length were inserted between the catalytic units. The specific activity of the galactose dehydrogenase part of the complex was increased when longer linkers (9 and 13 amino acids) were used as connectors. These bifunctional enzymes were predominantly found to comprise hexamers, however, complexes of higher molecular weight were also formed. The sequential reaction was carried out more efficiently when hybrid enzymes with the longer linkers were used as demonstrated both in vitro by using purified protein preparations as well as in vivo by determining the growth rates of recombinant E. coli cells on a minimal medium containing lactose.

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keywords
Amino Acid Sequence, Base Sequence, Chromatography, Gel, Cloning, Molecular, Enzyme Stability, Escherichia coli, Galactose, Galactose Dehydrogenases, Hydrogen-Ion Concentration, Kinetics, Lactose, Molecular Sequence Data, Molecular Weight, Multienzyme Complexes, NAD, Peptides, Protein Conformation, Recombinant Fusion Proteins, Temperature, beta-Galactosidase
in
Biochimica et Biophysica Acta
volume
1293
issue
1
pages
7 pages
publisher
Elsevier
external identifiers
  • scopus:0029887939
ISSN
0006-3002
DOI
10.1016/0167-4838(95)00240-5
language
English
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yes
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17370ed1-8045-475f-8761-d35bc5fc6a97
date added to LUP
2016-04-18 16:02:22
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2017-05-02 19:34:43
@article{17370ed1-8045-475f-8761-d35bc5fc6a97,
  abstract     = {<p>To examine the role of the connecting region in the artificial bifunctional enzyme beta-galactosidase/galactose dehydrogenase, linkers of different length were inserted between the catalytic units. The specific activity of the galactose dehydrogenase part of the complex was increased when longer linkers (9 and 13 amino acids) were used as connectors. These bifunctional enzymes were predominantly found to comprise hexamers, however, complexes of higher molecular weight were also formed. The sequential reaction was carried out more efficiently when hybrid enzymes with the longer linkers were used as demonstrated both in vitro by using purified protein preparations as well as in vivo by determining the growth rates of recombinant E. coli cells on a minimal medium containing lactose.</p>},
  author       = {Ljung, Sarah and Bülow, L and Carlsson, Hélen },
  issn         = {0006-3002},
  keyword      = {Amino Acid Sequence,Base Sequence,Chromatography, Gel,Cloning, Molecular,Enzyme Stability,Escherichia coli,Galactose,Galactose Dehydrogenases,Hydrogen-Ion Concentration,Kinetics,Lactose,Molecular Sequence Data,Molecular Weight,Multienzyme Complexes,NAD,Peptides,Protein Conformation,Recombinant Fusion Proteins,Temperature,beta-Galactosidase},
  language     = {eng},
  month        = {03},
  number       = {1},
  pages        = {60--154},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta},
  title        = {Physical and kinetic effects on induction of various linker regions in beta-galactosidase/galactose dehydrogenase fusion enzymes},
  url          = {http://dx.doi.org/10.1016/0167-4838(95)00240-5},
  volume       = {1293},
  year         = {1996},
}