4.1.3.25: (S)-citramalyl-CoA lyase
This is an abbreviated version!
For detailed information about (S)-citramalyl-CoA lyase, go to the full flat file.
Word Map on EC 4.1.3.25
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4.1.3.25
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itaconate
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hydratase
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succinate
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citramalate
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aeruginosa
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terreus
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yersinia
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succinyl-coa
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c5-dicarboxylic
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pestis
- 4.1.3.25
- itaconate
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hydratase
- succinate
- citramalate
- aeruginosa
- terreus
- yersinia
- succinyl-coa
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c5-dicarboxylic
- pestis
Reaction
Synonyms
(3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase, (3S)-citramalyl-CoA pyruvate-lyase, (S)-citramalyl-CoA lyase, CCL, CclA, CitE-like protein, citramalyl coenzyme A lyase, citramalyl-CoA lyase, citramalyl-thio-acyl carrier protein lyase, D-citramalyl-CoA lyase, lyase, citramalyl coenzyme A, malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase, MCL, MCLC, More, YpCcl
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General Information on EC 4.1.3.25 - (S)-citramalyl-CoA lyase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
physiological function
additional information
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
evolution
the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases)
evolution
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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
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
metabolism
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the enzyme catalyzes the last step of the itaconate degradation pathway
metabolism
the enzyme catalyzes the last step of the itaconate degradation pathway
metabolism
the enzyme catalyzes three different steps in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation, the tri-functionality of the MCLC underscores its key role for this pathway
metabolism
the enzyme is involved in the catabolic pathway of itaconic acid
metabolism
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the enzyme is involved in the degradation of itaconate
metabolism
the enzyme is involved in the itaconic acid degrading pathway in itaconic acid producing Aspergillus terreus
metabolism
Paraburkholderia xenovorans DSMZ 17367 / LB400
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the enzyme is involved in the degradation of itaconate
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metabolism
Aspergillus terreus LYT10
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the enzyme is involved in the catabolic pathway of itaconic acid
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metabolism
Aspergillus terreus LYT10
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the enzyme is involved in the itaconic acid degrading pathway in itaconic acid producing Aspergillus terreus
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physiological function
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the enzyme is crucial for survival of the pathogen in host macrophages
physiological function
the enzyme is crucial for survival of the pathogen in host macrophages
physiological function
the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus
physiological function
Chloroflexus aurantiacus OK-70-fl / DSM 636
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the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus
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