Lysine decarboxylase assay with cucurbituril (cucurbit-7-uril)

2007 ◽  
Author(s):  
Andreas Hennig ◽  
Hüseyin Bakirci ◽  
Werner M. Nau
Keyword(s):  
Lysine Decarboxylase

scholarly journals A Pathoadaptive Deletion in an Enteroaggregative Escherichia coli Outbreak Strain Enhances Virulence in a Caenorhabditis elegans Model

2010 ◽  
Vol 78 (9) ◽  
pp. 4068-4076 ◽  
Author(s):  
Jennifer Hwang ◽  
Lisa M. Mattei ◽  
Laura G. VanArendonk ◽  
Philip M. Meneely ◽  
Iruka N. Okeke
Keyword(s):  
Escherichia Coli ◽  
Caenorhabditis Elegans ◽  
Epithelial Cells ◽  
Genetic Material ◽  
Decarboxylase Activity ◽  
Multicopy Plasmid ◽  
Lysine Decarboxylase ◽  
Outbreak Strain ◽  
E Coli ◽  
C Elegans

ABSTRACT Enteroaggregative Escherichia coli (EAEC) strains are important diarrheal pathogens. EAEC strains are defined by their characteristic stacked-brick pattern of adherence to epithelial cells but show heterogeneous virulence and have different combinations of adhesin and toxin genes. Pathoadaptive deletions in the lysine decarboxylase (cad) genes have been noted among hypervirulent E. coli subtypes of Shigella and enterohemorrhagic E. coli. To test the hypothesis that cad deletions might account for heterogeneity in EAEC virulence, we developed a Caenorhabditis elegans pathogenesis model. Well-characterized EAEC strains were shown to colonize and kill C. elegans, and differences in virulence could be measured quantitatively. Of 49 EAEC strains screened for lysine decarboxylase activity, 3 tested negative. Most notable is isolate 101-1, which was recovered in Japan, from the largest documented EAEC outbreak. EAEC strain 101-1 was unable to decarboxylate lysine in vitro due to deletions in cadA and cadC, which, respectively, encode lysine decarboxylase and a transcriptional activator of the cadAB genes. Strain 101-1 was significantly more lethal to C. elegans than control strain OP50. Lethality was attenuated when the lysine decarboxylase defect was complemented from a multicopy plasmid and in single copy. In addition, restoring lysine decarboxylase function produced derivatives of 101-1 deficient in aggregative adherence to cultured human epithelial cells. Lysine decarboxylase inactivation is pathoadapative in an important EAEC outbreak strain, and deletion of cad genes could produce hypervirulent EAEC lineages in the future. These results suggest that loss, as well as gain, of genetic material can account for heterogeneous virulence among EAEC strains.

In situ immobilization of lysine decarboxylase on a biopolymer by fusion with phasin

2016 ◽  
Vol 51 (10) ◽  
pp. 1413-1419 ◽  
Author(s):  
Hyung-Min Seo ◽  
Jung-Ho Kim ◽  
Jong-Min Jeon ◽  
Hun-Suk Song ◽  
Shashi Kant Bhatia ◽  
...  
Keyword(s):  
Lysine Decarboxylase ◽  
In Situ Immobilization

Production of Cadaverine in Recombinant Corynebacterium Glutamicum Overexpressing Lysine Decarboxylase (ldcC) and Response Regulator dr1558

2021 ◽  
Author(s):  
Soong-bin Kang ◽  
Jong-il choi
Keyword(s):  
Corynebacterium Glutamicum ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Deinococcus Radiodurans ◽  
Response Regulator ◽  
Fold Increase ◽  
Lysine Biosynthesis ◽  
Lysine Decarboxylase ◽  
Fed Batch ◽  
Fed Batch Fermentation ◽  
Polymerase Chain

Abstract In this study, the response regulator DR1558 from Deinococcus radiodurans was overexpressed in recombinant Corynebacterium glutamicum with lysine decarboxylase (ldcC). The recombinant C. glutamicum strain overexpressing dr1558 and ldcC produced 5.9 g/L of cadaverine by flask cultivation, whereas the control strain overexpressing only ldcC produced 4.5 g/L of cadaverine. To investigate the mechanism underlying the effect of DR1558, the expression levels of genes related to central metabolism and lysine-biosynthesis were analyzed by quantitative-real time polymerase chain reaction. The results showed that phosphoenolpyruvate carboxykinase (pck) was downregulated, and pyruvate kinase (pyk) and other lysine biosynthesis genes were upregulated. Furthermore, in fed-batch fermentation, C. glutamicum coexpressing dr1558 produced 25.14 g/L of cadaverine, a 1.25-fold increase in concentration relative to the control. These results suggested that the heterologous expression of dr1558 may improve the production of biorefinery products by recombinant C. glutamicum.

Lysine decarboxylase

1990 ◽  
pp. 67-70
Author(s):  
Dietmar Schomburg ◽  
Margit Salzmann
Keyword(s):  
Lysine Decarboxylase

Optimization of Direct Lysine Decarboxylase Biotransformation for Cadaverine Production with Whole-Cell Biocatalysts at High Lysine Concentration

2015 ◽  
Vol 25 (7) ◽  
pp. 1108-1113 ◽  
Author(s):  
Hyun Joong Kim ◽  
Yong Hyun Kim ◽  
Ji-Hyun Shin ◽  
Shashi Kant Bhatia ◽  
Ganesan Sathiyanarayanan ◽  
...  
Keyword(s):  
Lysine Decarboxylase ◽  
Whole Cell ◽  
High Lysine ◽  
Lysine Concentration

scholarly journals High-Level Conversion of l-lysine into Cadaverine by Escherichia coli Whole Cell Biocatalyst Expressing Hafnia alvei l-lysine Decarboxylase

Polymers ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 1184 ◽  
Author(s):  
Kim ◽  
Baritugo ◽  
Oh ◽  
Kang ◽  
Jung ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Expression ◽  
Pyridoxal Phosphate ◽  
Lysine Decarboxylase ◽  
Hafnia Alvei ◽  
Whole Cell ◽  
E Coli ◽  
Whole Cell Biocatalyst ◽  
High Level ◽  
Whole Cell Bioconversion

Cadaverine is a C5 diamine monomer used for the production of bio-based polyamide 510. Cadaverine is produced by the decarboxylation of l-lysine using a lysine decarboxylase (LDC). In this study, we developed recombinant Escherichia coli strains for the expression of LDC from Hafnia alvei. The resulting recombinant XBHaLDC strain was used as a whole cell biocatalyst for the high-level bioconversion of l-lysine into cadaverine without the supplementation of isopropyl β-d-1-thiogalactopyranoside (IPTG) for the induction of protein expression and pyridoxal phosphate (PLP), a key cofactor for an LDC reaction. The comparison of results from enzyme characterization of E. coli and H. alvei LDC revealed that H. alvei LDC exhibited greater bioconversion ability than E. coli LDC due to higher levels of protein expression in all cellular fractions and a higher specific activity at 37 °C (1825 U/mg protein > 1003 U/mg protein). The recombinant XBHaLDC and XBEcLDC strains were constructed for the high-level production of cadaverine. Recombinant XBHaLDC produced a 1.3-fold higher titer of cadaverine (6.1 g/L) than the XBEcLDC strain (4.8 g/L) from 10 g/L of l-lysine. Furthermore, XBHaLDC, concentrated to an optical density (OD600) of 50, efficiently produced 136 g/L of cadaverine from 200 g/L of l-lysine (97% molar yield) via an IPTG- and PLP-free whole cell bioconversion reaction. Cadaverine synthesized via a whole cell biocatalyst reaction using XBHaLDC was purified to polymer grade, and purified cadaverine was successfully used for the synthesis of polyamide 510. In conclusion, an IPTG- and PLP-free whole cell bioconversion process of l-lysine into cadaverine, using recombinant XBHaLDC, was successfully utilized for the production of bio-based polyamide 510, which has physical and thermal properties similar to polyamide 510 synthesized from chemical-grade cadaverine.

Biofilm Lysine Decarboxylase, a New Therapeutic Target for Periodontal Inflammation

2015 ◽  
Vol 86 (10) ◽  
pp. 1176-1184 ◽  
Author(s):  
Zsolt Lohinai ◽  
Beata Keremi ◽  
Eva Szöko ◽  
Tamás Tábi ◽  
Csaba Szabo ◽  
...  
Keyword(s):  
Therapeutic Target ◽  
Lysine Decarboxylase ◽  
Periodontal Inflammation
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