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Results 1 - 10 of 16 > >>
EC Number
General Information
Commentary
Reference
evolution
certain enterobacteria exert evolutionary pressure on the lysine decarboxylase towards the macromolecular cage-like assembly with AAA+ ATPase RavA, implying that this complex may have an important function under particular stress conditions. The C-terminal beta-sheet of a lysine decarboxylase is a highly conserved signature allowing to distinguish between LdcI and LdcC. RavA is binding to LdcI, but is not capable of binding to LdcC, LDC sequence comparisons and phylogenetic analysis; certain enterobacteria exert evolutionary pressure on the lysine decarboxylase towards the macromolecular cage-like assembly with AAA+ ATPase RavA, implying that this complex may have an important function under particular stress conditions. The C-terminal beta-sheet of a lysine decarboxylase is a highly conserved signature allowing to distinguish between LdcI and LdcC. RavA is binding to LdcI, but is not capable of binding to LdcC, LDC sequence comparisons and phylogenetic analysis
evolution
Selenomonas ruminantium SrLDC shows much lower pyridoxal 5'-phosphate affinity than other pyridoxal 5'-phosphate-dependent enzymes. The highly flexible active site contributes to the low affinity for pyridoxal 5'-phosphate in SrLDC
evolution
the L-lysine decarboxylase (LDC) genes from Escherichia coli include genes cadA and ldcC encoding the acid-inducible enzyme CadA and the constitutive LDCc, respectively
metabolism
changes in the contents of plant biogenic amines (putrescine, cadaverine, spermidine, tryptamine, spermine and histamine) and key enzymes of their biosynthesis, i.e. lysine decarboxylase (LDC), tyrosine decarboxylase, and ornithine decarboxylase (ODC) in galls and other parts of Siberian elm (Ulmus pumila) leaves during the galling process caused by the aphid Tetraneura ulmi first instar larvae, overview
more
compared to the activity of lysine/ornithine decarboxylase from Selenomonas ruminantium and from Vibrio vulnificus, the cadaverine producing activity of enzyme gtLDC is severalfold reduced
more
construction of a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and yo-electron microscopy 3D reconstructions of the Escherichia coli LdcI and LdcC at optimal pH, overview. RavA is not capable of binding to LdcC. Conformational rearrangements in the enzyme LdcI active site, overview; Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC
more
due to the flexible pyridoxal 5'-phosphate binding site, the protein undergoes an open/closed conformational change at the PLP binding site depending on the pyridoxal 5'-phosphate binding. Especially, two loops located in the vicinity of the pyridoxal 5'-phosphate binding site, the pyridoxal 5'-phosphate stabilization loop (PS-loop) and the regulatory loop (R-loop), undergo a significant structural movement depending on the pyridoxal 5'-phosphate binding
more
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
more
structure of enzyme SrLDC in complex with pyridoxal 5'-phosphate and cadaverine and binding mode of cofactor and substrate, overview
more
the LDC monomer has a C-terminal domain (residues 564-715), that has a predominantly alpha-helical outer surface and an inner surface that consists of two sets of beta-sheets, and is very important. The C-terminal domain forms part of the entry channel into the active site of the enzyme. The amino acid change E583G changes a residue located in this channel with improving effects on enzyme activity
Results 1 - 10 of 16 > >>