Copper homeostasis protein CutC was originally thought to be involved in copper tolerance in Escherichia coli, as mutation in the corresponding gene lead to an increased copper sensitivity []. However, this phenotype has been later reported to depend on the levels of the mRNA-interfering complementary RNA regulator MicL, which is transcribed from a promoter located within the coding sequence of the cutC gene in the enterobacteria []. In the plant pathogen Xylella fastidiosa, this protein has been reported as specific for copper efflux []. The structure of this protein in the bacteria Shigella flexneri showed a monomer structure that adopts a common TIM β/α barrel with 8 β-strands surrounded by 8 α-helices [].The human homologue of this protein, which structure showed a potential copper-binding site, has an important role in intracellular copper homeostasis [, ].
A gene cluster responsible for anaerobic choline degradation has been identified within the genome of sulfate-reducing bacteria. The choline utilisation (cut) gene cluster consist of cutC and cutD. Members of this family are CutD, a radical enzyme that serves as an activase for choline TMA-lyase, CutC. CutC is a glycyl radical enzyme related to pyruvate formate-lyase. CutD is related to pyruvate formate-lyase activase [].
Copper homeostasis protein CutC was originally thought to be involved in copper tolerance in Escherichia coli, as mutation in the corresponding gene lead to an increased copper sensitivity []. However, this phenotype has been later reported to depend on the levels of the mRNA-interfering complementary RNA regulator MicL, which is transcribed from a promoter located within the coding sequence of the cutC gene in the enterobacteria []. In the plant pathogen Xylella fastidiosa, this protein has been reported as specific for copper efflux []. The structure of this protein in the bacteria Shigella flexneri showed a monomer structure that adopts a common TIM β/α barrel with 8 β-strands surrounded by 8 α-helices [].The human homologue of this protein, which structure showed a potential copper-binding site, has an important role in intracellular copper homeostasis [, ].
This group of enzymes are activating enzymes (activases) and include:Pyruvate formate-lyase-activating enzyme (PflA, ), which activates pyruvate formate-lyase under anaerobic conditions using S-adenosylmethionine and reduced flavodoxin as cosubstrates [].4-hydroxyphenylacetate decarboxylase activating enzyme (HpdA), which activates 4-hydroxyphenylacetate decarboxylase under anaerobic conditions [].Benzylsuccinate synthase activating enzyme (BssD), which activates benzylsuccinate synthase under anaerobic conditions using S-adenosylmethionine and reduced flavodoxin as cosubstrates [].Choline trimethylamine-lyase activating enzyme (CutD), which activates choline trimethylamine-lyase CutC under anaerobic conditions [].Putative glycyl-radical enzyme activating enzyme YjjW.Trans-4-hydroxy-L-proline dehydratase activating enzyme PflE []. Isethionate sulfite-lyase activating enzyme IslB [].
