EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.3.25 | Mg2+ | required | Clostridium tetanomorphum | |
4.1.3.25 | Mg2+ | the isolated beta-subunit of citramalate lyase becomes saturated at 10 mM Mg2+ | Clostridium tetanomorphum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.3.11 | acetyl-[acyl-carrier protein] + citramalate | Clostridium tetanomorphum | biological significant reaction, alpha-subunit of citramalate lyase enzyme complex | citramalyl-[acyl-carrier protein] + acetate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.8.3.11 | Clostridium tetanomorphum | - |
alpha-subunit of the citramalate enzyme complex | - |
4.1.3.22 | Clostridium tetanomorphum | - |
- |
- |
4.1.3.25 | Clostridium tetanomorphum | - |
EC 4.1.3.25 is the beta-subunit of EC 4.1.3.22 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.8.3.11 | - |
Clostridium tetanomorphum |
EC Number | Renatured (Comment) | Organism |
---|---|---|
2.8.3.11 | reconstitution of the enzyme complex at pH 8.0, 25°C | Clostridium tetanomorphum |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.8.3.11 | additional information | - |
- |
Clostridium tetanomorphum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.3.11 | acetyl-CoA + citramalate | alpha-subunit of the citramalate enzyme complex | Clostridium tetanomorphum | acetate + (3S)-citramalyl-CoA | - |
r | |
2.8.3.11 | acetyl-[acyl-carrier protein] + citramalate | substrate is the acetylated acyl carrier protein of citrate lyase or citramalate lyase enzyme complex | Clostridium tetanomorphum | citramalyl-[acyl-carrier protein] + acetate | - |
? | |
2.8.3.11 | acetyl-[acyl-carrier protein] + citramalate | biological significant reaction, alpha-subunit of citramalate lyase enzyme complex | Clostridium tetanomorphum | citramalyl-[acyl-carrier protein] + acetate | - |
? | |
2.8.3.11 | additional information | no substrate: citrate | Clostridium tetanomorphum | ? | - |
? | |
2.8.3.11 | additional information | also catalyses citramalate dependent exchange reaction between acetate and acetyl-CoA | Clostridium tetanomorphum | ? | - |
? | |
4.1.3.22 | citramalate | the alpha-subunit catalyzes the formation of acetyl-CoA and citramalate. The beta-subunit catalyzes the cleavage of (3S)-citramalyl-thio-acyl carrier protein lyase | Clostridium tetanomorphum | acetate + pyruvate | - |
? | |
4.1.3.25 | (3S)-citramalyl-thio-acylcarrier protein | - |
Clostridium tetanomorphum | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.3.22 | oligomer | the alpha-subunit represents an acetyl-thio-acyl carrier protein:citramalate acyl carrier protein transferase and the beta-subunit a (3S)-citramalyl-thio-acyl carrier protein lyase | Clostridium tetanomorphum |
4.1.3.25 | More | EC 4.1.3.25 is the beta-subunit of EC 4.1.3.22 | Clostridium tetanomorphum |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.3.25 | More | EC 4.1.3.25 is the beta-subunit of EC 4.1.3.22 | Clostridium tetanomorphum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.8.3.11 | 25 | - |
assay at | Clostridium tetanomorphum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.8.3.11 | 8 | - |
assay at | Clostridium tetanomorphum |