Recombinant Mycobacterium ulcerans Succinyl-CoA ligase [ADP-forming] subunit beta (sucC)
Description
Enzymatic Function and Biological Role
Succinyl-CoA ligase (SCS) catalyzes the reversible conversion of succinyl-CoA and ADP to succinate and ATP in the Krebs cycle. The beta subunit (SucC) determines substrate specificity for ADP. In M. ulcerans, this enzyme likely supports energy metabolism and biosynthetic precursor generation, critical for survival in low-oxygen environments like necrotic skin lesions.
Key Observations:
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SCS deficiency in humans (linked to SUCLA2 mutations) causes mitochondrial DNA depletion and metabolic disorders .
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M. ulcerans relies on unique virulence factors like mycolactone, a cytotoxic macrolide synthesized by plasmid-encoded polyketide synthases (PKS) . While SucC is not directly involved in mycolactone production, its role in central metabolism may indirectly support toxin biosynthesis by supplying ATP or succinate.
Research Applications and Challenges
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Vaccine Development: Recombinant antigens like MUL2232 and MUL3720 from M. ulcerans have been tested in murine models, though protective efficacy remains limited .
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Metabolic Pathways: M. ulcerans exhibits metabolic flexibility, utilizing host-derived lipids during infection. SCS activity might facilitate adaptation to nutrient stress .
Unresolved Questions and Future Directions
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Does SucC interact with other virulence factors, such as mycolactone?
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Could targeting SCS disrupt M. ulcerans persistence in human tissue?
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Comparative studies with human SUCLA2 may reveal pathogen-specific therapeutic targets.
Product Specs
Target Background
KEGG: mul:MUL_4720
