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Literature summary extracted from

  • Erbilgin, O.; Sutter, M.; Kerfeld, C.A.
    The structural basis of coenzyme A recycling in a bacterial organelle (2016), PLoS Biol., 14, e1002399 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.222 expression in Escherichia coli BL21(DE3) Rhodopseudomonas palustris
2.3.1.222 expression in Escherichia coli BL21(DE3) Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.222 crystals are obtained from sitting drop experiments at 22°C. High-resolution PduL crystal structures with bound substrates. The PduL fold is unrelated to that of Pta. It contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping phosphotransacylase (PTAC) Rhodopseudomonas palustris

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.222 Rhodopseudomonas palustris Q21A54
-
-
2.3.1.222 Rhodopseudomonas palustris BisB18 Q21A54
-
-
2.3.1.222 Salmonella enterica subsp. enterica serovar Typhimurium Q9XDN5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.222
-
 Rhodopseudomonas palustris
2.3.1.222
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.222 propanoyl-CoA + phosphate
-
 Rhodopseudomonas palustris CoA + propanoyl phosphate
-
 ?
2.3.1.222 propanoyl-CoA + phosphate
-
 Salmonella enterica subsp. enterica serovar Typhimurium CoA + propanoyl phosphate
-
 ?
2.3.1.222 propanoyl-CoA + phosphate
-
 Rhodopseudomonas palustris BisB18 CoA + propanoyl phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.222 PduL
-
 Rhodopseudomonas palustris
2.3.1.222 PduL
-
 Salmonella enterica subsp. enterica serovar Typhimurium

General Information

EC Number General Information Comment Organism
2.3.1.222 evolution the phosphotransacylase (PTAC) predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). PduL and Pta exemplify functional, but not structural, convergent evolution Rhodopseudomonas palustris
2.3.1.222 evolution the phosphotransacylase (PTAC) predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). PduL and Pta exemplify functional, but not structural, convergent evolution Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.222 metabolism the fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt bacterial microcompartments(BMC)-based metabolism, while not affecting most commensal organisms that require phosphotransacylase (PTAC) activity Rhodopseudomonas palustris
2.3.1.222 metabolism the fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt bacterial microcompartments(BMC)-based metabolism, while not affecting most commensal organisms that require phosphotransacylase (PTAC) activity Salmonella enterica subsp. enterica serovar Typhimurium