EC Number   |
General Information |
Reference |
|---|
   2.3.2.3 | evolution |
according to the presence of IS6110 insertion in the NTF region, the Beijing genotype is currently divided into two subtypes. The ancient subtype is characterized with the intact NTF region, whereas modern subtype strains demonstrate the presentation of IS6110 insertion in the NTF region. The latter subtype strains can also be discriminated by the polymorphisms of mutT genes. Modern subtype is designated to Beijing monophyletic groups 3 (Bj-MG3), whereas ancient subtype is further subdivided into Bj-MG1 and Bj-MG2 based on the RD181 deletion. The strains of modern subtype constitute the majority of Beijing genotype in most regions and demonstrate an increased virulent phenotype |
-, 758524 |
| 2.3.2.3 | evolution |
the enzyme belongs to the LysX family of enzymes. Analysis of the mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities, overview. Substrate recognition mechanism in LysX family proteins. The lysX homologues in the lysine biosynthetic gene cluster encode enzymes that possess the signature motif (Tyr175, Ile185, Thr196, and Asn250-Ala251) for the LysX/ArgX bifunctional enzyme |
-, 745351 |
| 2.3.2.3 | malfunction |
a MprF knockout mutant demonstrates a substantial increase in the phosphatidylglycerol:lysylphosphatidylglycerol ratio of the membrane |
720483 |
| 2.3.2.3 | malfunction |
a Mycobacterium avium lysX mutant strain undergoes a transition in phenotype by switching the carbon metabolism to beta-oxidation of fatty acids, along with accumulation of lipid inclusions. Proteins associated with intracellular survival are upregulated in the lysX mutant, even during extracellular growth, preparing bacteria for the conditions occurring inside host cells. In line with this, the lysX mutant exhibits enhanced intracellular growth in human-blood-derived monocytes |
-, 757359 |
| 2.3.2.3 | malfunction |
gain-of-function mutations in the phospholipid flippase MprF confer specific daptomycin resistance, although the T345A mutation does not alter lysyl-phosphatidylglycerol (LysPG) synthesis, LysPG translocation, or the Staphylococcus aureus cell surface charge. MprF-mediated DAP-resistance relies on a functional flippase domain and is restricted to daptomycin and a related cyclic lipopeptide antibiotic, friulimicin B. Daptomycin-resistant (DAP-R) Staphylococcus aureus mutants emerge during therapy, featuring isolates which in most cases possess point mutations in the mprF gene. T345A is a naturally occuring single nucleotide polymorphism (SNP) that can reproducibly cause daptomycin resistance, the mutation leads to weakened intramolecular domain interactions of MprF, suggesting that daptomycin and friulimicin resistance-conferring mutations may alter the substrate range of the MprF flippase to directly translocate these lipopeptide antibiotics or other membrane components with crucial roles in the activity of these antimicrobials |
757555 |
| 2.3.2.3 | malfunction |
identification of lysX mutants, Beijing and modern Beijing strains, genotyping, overview. Beijing family is a genotype of Mycobacterium tuberculosis that is disseminated worldwide predominating throughout East Asia, the former Soviet Union and South Africa. This family has a common spoligotype signature and lack of the region of difference (RD) 105. Clinical and epidemiological studies demonstrate that Beijing genotype strains are associated with high levels of bacterial resistance to drugs and enhanced ability to cause disease, contributing to increased transmissibility and rapid progression from infection to active disease. Evaluation of the virulence of Beijing genotype strains shows a wide range of virulence phenotypes |
-, 758524 |
| 2.3.2.3 | metabolism |
significance of lysX in the metabolism and virulence of the environmental pathogen Mycobacterium avium hominissuis |
-, 757359 |
| 2.3.2.3 | metabolism |
the C-terminal domain of the enzyme is responsible for the synthesis of lysylphosphatidylglycerol |
720483 |
| 2.3.2.3 | metabolism |
the enzyme LysX is involved in the lysine biosynthesis pathway. The conversion from alpha-aminoadipate (AAA) to lysine, is accomplished by five enzymes: LysX, LysZ, LysY, LysJ, and LysK, using the amino group carrier protein LysW. The alpha-amino group of AAA is modified with LysW by LysX, forming an isopeptide bond between the alpha-amino group of AAA and gamma-carboxyl group of the glutamate residue at the C terminus of LysW. LysW-gamma-AAA thus synthesized is then transferred to subsequent biosynthetic enzymes to be converted to LysW-gamma-lysine by phosphorylation, reduction, and amination steps. In the final step, LysW-gamma-lysine is recognized by LysK, a carboxypeptidase, resulting in the release of lysine. LysW contains many acidic amino acid residues for electrostatic interactions with each enzyme, and, thus, functions as an amino group carrier protein for efficient lysine biosynthesis |
-, 745351 |
| 2.3.2.3 | more |
compound determination by mass spectrometry |
-, 757073 |
