EC Number   |
Protein Variants |
Reference |
|---|
    4.1.1.18 | more |
a lack of cadaverine caused by mutation in cadA results in low tolerance to oxidative stress compared to the wild type, cadaverine, which neutralizes the external medium, also appears to scavenge superoxide radicals, since increasing cellular cadaverine by elevating the gene dosage of cadBA significantly diminished the induction of Mn-containing superoxide dismutase under methyl viologen-induced oxidative stress, overview |
680477 |
| 4.1.1.18 | more |
biotransformation of cadaverine using a lysine decarboxylase from Klebsiella oxytoca expressed in Escherichia coli. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli, which leads to a system that converts more than 24% lysine-HCl to cadaverine compared to the same system expressing CadA, overview. The final optimized system converts lysine-HCl to cadaverine at a conversion rate of 0.133%/min/g |
-, 747357 |
| 4.1.1.18 | more |
cadaverine is a major source of many industrial polyamides such as nylon and chelating agents. Cadaverine is produced by the microbial fermentation of glucose to lysine, which is then decarboxylated by lysine decarboxylase CadA. But utilizing CadA for cadaverine production causes enzyme instability. In order to stabilize the CadA homodecamer structure for in vitro decarboxylation reaction, four disulfide bond mutants in the multimeric interfacial region are designed, CadA plasmid library/mutant screening |
-, 747369 |
| 4.1.1.18 | more |
construction of a cadA gene-inactivated strain from wild-type strain V02-64, serotype O3:K, by a plasmid integrated in its chromosome, single crossing over, acid resistance of the mutant strain at pH 4.0 in phosphate buffer is weaker than in the parental strain |
680417 |
| 4.1.1.18 | more |
development of an innovative immobilisation approach using catalytically active recombinant constitutive L-lysine decarboxylase (EcLDCc) in inclusion bodies, CatIBs, overview. EcLDCc-CatIBs can compete with the whole cell biocatalyst in production of cadaverine |
749366 |
| 4.1.1.18 | more |
directed evolution of LDC and high-throughput mutant screening, mutant library construction using DNA shuffling or error-prone PCR (optimum concentrations of Mn2+ and Mg2+ are 5 and 0.2 mM, respectively). Three nucleotide mutations, A438G, G439T, and A1748G correspond to amino acid changes V147F and E583G |
-, 747358 |
| 4.1.1.18 | more |
disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity |
749101 |
| 4.1.1.18 | more |
engineering the decameric interface for potential for industrial applications |
747396 |
| 4.1.1.18 | more |
identification of mutant Ldc-co with increased lysine decarboxylase ability. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli. Identification of mutant lysine decarboxylase enzymes with enhanced cadaverine-production ability. Together, these modifications increase cadaverine production in the system by 50%, and the system has a yield of 80% from lysine-HCl, the system to produce cadaverine using the lysine decarboxylase from Klebsiella oxytoca performs at a level that is competitive with the traditional systems using the Escherichia coli lysine decarboxylases in both lab-scale and batch fermentation conditions. Generation of several mutant strains and evaluation, overview |
-, 747655 |
| 4.1.1.18 | more |
immobilization of the recombinant enzyme CadA, preparation of a cross-linked enzyme aggregate (CLEA) of Escherichia coli CadA and bioconversion of lysine using CadACLEA. The thermostability of CadACLEA is significantly higher than that of CadAfree. The optimum temperatures of CadAfree and CadACLEA are 60°C and 55°C, respectively. The thermostability of CadACLEA is significantly higher than that of CadAfree. The optimum pH of both enzymes is 6.0. CadAfree cannot be recovered after use, whereas CadACLEA is rapidly recovered and the residual activity is 53% after the 10th recycle |
748386 |
