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Literature summary for 4.1.3.25 extracted from

  • Sasikaran, J.; Ziemski, M.; Zadora, P.K.; Fleig, A.; Berg, I.A.
    Bacterial itaconate degradation promotes pathogenicity (2014), Nat. Chem. Biol., 10, 371-377.
    View publication on PubMed
Search for more literature for 4.1.3.25

Cloned(Commentary)

Cloned (Comment) Organism
gene ccl or PA0883 , genetic structure, the enzyme is encoded in a six-gene operon Pseudomonas aeruginosa
gene ccl or Y2383 or ripC, genetic structure, the enzyme is encoded in a three-gene operon, in vitro reconstitution of itaconate degradation pathway with the heterologously produced and purified enzymes from Yersinia pestis Yersinia pestis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Pseudomonas aeruginosa
Mg2+ activates Yersinia pestis
Mg2+ activates Pseudomonas aeruginosa
Mn2+ activates Yersinia pestis
Mn2+ activates Pseudomonas aeruginosa
additional information activity of YpCcl is dependent on the presence of divalent cations such as Mg2+ or Mn2+ Yersinia pestis
additional information the enzyme PaCcl requires divalent metal ions, such as Mg2+, Mn2+ or Co2+, for activity Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-citramalyl-CoA Yersinia pestis
-
 acetyl-CoA + pyruvate
-
 ?
(S)-citramalyl-CoA Pseudomonas aeruginosa
-
 acetyl-CoA + pyruvate
-
 ?
(S)-citramalyl-CoA Yersinia pestis Y2384
-
 acetyl-CoA + pyruvate
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9I562 gene ccl or PA0883
-
Yersinia pestis
-
 gene ccl or Y2383 or ripC
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-citramalyl-CoA
-
 Yersinia pestis acetyl-CoA + pyruvate
-
 ?
(S)-citramalyl-CoA
-
 Pseudomonas aeruginosa acetyl-CoA + pyruvate
-
 ?
(S)-citramalyl-CoA
-
 Yersinia pestis Y2384 acetyl-CoA + pyruvate
-
 ?
additional information PaCcl is highly specific for its substrate, (S)-citramalyl-CoA. It also catalyzes stereospecifically the (R)-3-hydroxy-3-methylglutaryl-CoA lyase reaction and the (3S)-citryl-CoA lyase reaction, EC 4.1.3.34, albeit with much lower catalytic efficiency. No activity with (S)-3-hydroxy-3-methylglutaryl-CoA Pseudomonas aeruginosa ?
-
 ?
additional information YpCcl does not accept other tested beta-hydroxyacyl-CoA compounds, such as 3-hydroxy-3-methylglutaryl-CoA, (3S)-malyl-CoA or beta-methylmalyl-CoA as substrates, but it catalyzes the (3S)-citryl-CoA lyase reaction, EC 4.1.3.34, albeit with lower catalytic efficiency Yersinia pestis ?
-
 ?
additional information YpCcl does not accept other tested beta-hydroxyacyl-CoA compounds, such as 3-hydroxy-3-methylglutaryl-CoA, (3S)-malyl-CoA or beta-methylmalyl-CoA as substrates, but it catalyzes the (3S)-citryl-CoA lyase reaction, EC 4.1.3.34, albeit with lower catalytic efficiency Yersinia pestis Y2384 ?
-
 ?

Synonyms

Synonyms Comment Organism
CCL
-
 Yersinia pestis
CCL
-
 Pseudomonas aeruginosa
CitE-like protein
-
 Yersinia pestis
CitE-like protein
-
 Pseudomonas aeruginosa
YpCcl
-
 Yersinia pestis

General Information

General Information Comment Organism
evolution the itaconate degradation and detoxification pathways of Yersinia and Pseudomonas, both possessing three genes for itaconate degradation, i.e. itaconate coenzyme A (CoA) transferase, itaconyl-CoA hydratase and (S)-citramalyl-CoA lyase, encoded in the rip operon, are the result of convergent evolution Yersinia pestis
evolution the itaconate degradation and detoxification pathways of Yersinia and Pseudomonas, both possessing three genes for itaconate degradation, i.e. itaconate coenzyme A (CoA) transferase, itaconyl-CoA hydratase and (S)-citramalyl-CoA lyase, encoded in the rip operon, are the result of convergent evolution Pseudomonas aeruginosa
metabolism the enzyme catalyzes the last step of the itaconate degradation pathway Yersinia pestis
metabolism the enzyme catalyzes the last step of the itaconate degradation pathway Pseudomonas aeruginosa
physiological function the enzyme is crucial for survival of the pathogen in host macrophages Yersinia pestis
physiological function the enzyme is crucial for survival of the pathogen in host macrophages Pseudomonas aeruginosa