EC Number | Cloned (Comment) | Organism |
---|---|---|
4.4.1.13 | gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme TmCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form | Thermotoga maritima |
4.4.1.13 | gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme wMelCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form | Wolbachia pipientis |
4.4.1.13 | gene metC, phylogenetic analysis, the recombinant MBP-tagged enzyme PuCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Attempts to optimize recombinant production of the Pelagibacter ubique enzyme (PuCBL) in a soluble form are unsuccessful | Candidatus Pelagibacter ubique |
4.4.1.13 | gene metC, phylogenetic analysis. The recombinant enzyme EcCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially | Escherichia coli |
5.1.1.1 | gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme TmCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form | Thermotoga maritima |
5.1.1.1 | gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme wMelCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form | Wolbachia pipientis |
5.1.1.1 | gene metC, phylogenetic analysis, the recombinant MBP-tagged enzyme PuCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Attempts to optimize recombinant production of the Pelagibacter ubique enzyme (PuCBL) in a soluble form are unsuccessful | Candidatus Pelagibacter ubique |
5.1.1.1 | gene metC, phylogenetic analysis. The recombinant enzyme EcCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially | Escherichia coli |
5.1.1.3 | gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme TmCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form | Thermotoga maritima |
5.1.1.3 | gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme wMelCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form | Wolbachia pipientis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.4.1.13 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Candidatus Pelagibacter ubique | |
4.4.1.13 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Wolbachia pipientis | |
4.4.1.13 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Thermotoga maritima | |
4.4.1.13 | 0.02 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
4.4.1.13 | 0.4 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer | Thermotoga maritima | |
4.4.1.13 | 0.7 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
4.4.1.13 | 1.3 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima | |
4.4.1.13 | 2.1 | - |
cystathionine | recombinant MBP-tagged enzyme, pH 8.0, 37°C | Candidatus Pelagibacter ubique | |
5.1.1.1 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Candidatus Pelagibacter ubique | |
5.1.1.1 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Wolbachia pipientis | |
5.1.1.1 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Thermotoga maritima | |
5.1.1.1 | 0.38 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 3.8 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
5.1.1.1 | 4.2 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer | Thermotoga maritima | |
5.1.1.1 | 8.2 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 12 | - |
L-alanine | recombinant MBP-tagged enzyme, pH 8.0, 37°C | Candidatus Pelagibacter ubique | |
5.1.1.3 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Wolbachia pipientis | |
5.1.1.3 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Thermotoga maritima | |
5.1.1.3 | 0.26 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
5.1.1.3 | 0.8 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
5.1.1.3 | 1.4 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.4.1.13 | cystathionine + H2O | Escherichia coli | - |
L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | Candidatus Pelagibacter ubique | - |
L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | Wolbachia pipientis | - |
L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | Thermotoga maritima | - |
L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | Candidatus Pelagibacter ubique HTCC1062 | - |
L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | additional information | Wolbachia pipientis | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | ? | - |
- |
|
4.4.1.13 | additional information | Thermotoga maritima | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | ? | - |
- |
|
4.4.1.13 | additional information | Wolbachia pipientis wMel | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.1 | L-alanine | Escherichia coli | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Candidatus Pelagibacter ubique | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Wolbachia pipientis | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Thermotoga maritima | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Wolbachia pipientis wMel | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Candidatus Pelagibacter ubique HTCC1062 | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Thermotoga maritima DSM 3109 | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Thermotoga maritima ATCC 43589 | - |
D-alanine | - |
r | |
5.1.1.1 | L-alanine | Thermotoga maritima JCM 10099 | - |
D-alanine | - |
r | |
5.1.1.1 | additional information | Wolbachia pipientis | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.1 | additional information | Thermotoga maritima | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.1 | additional information | Wolbachia pipientis wMel | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.1 | additional information | Thermotoga maritima DSM 3109 | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.1 | additional information | Thermotoga maritima ATCC 43589 | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.1 | additional information | Thermotoga maritima JCM 10099 | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.3 | L-glutamate | Wolbachia pipientis | - |
D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | Thermotoga maritima | - |
D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | Wolbachia pipientis wMel | - |
D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | Thermotoga maritima DSM 3109 | - |
D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | Thermotoga maritima ATCC 43589 | - |
D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | Thermotoga maritima JCM 10099 | - |
D-glutamate | - |
r | |
5.1.1.3 | additional information | Wolbachia pipientis | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.3 | additional information | Thermotoga maritima | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.3 | additional information | Wolbachia pipientis wMel | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.3 | additional information | Thermotoga maritima DSM 3109 | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.3 | additional information | Thermotoga maritima ATCC 43589 | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
|
5.1.1.3 | additional information | Thermotoga maritima JCM 10099 | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | ? | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.4.1.13 | Candidatus Pelagibacter ubique | Q4FME3 | - |
- |
4.4.1.13 | Candidatus Pelagibacter ubique HTCC1062 | Q4FME3 | - |
- |
4.4.1.13 | Escherichia coli | P06721 | - |
- |
4.4.1.13 | Thermotoga maritima | Q9X0Z7 | - |
- |
4.4.1.13 | Thermotoga maritima ATCC 43589 | Q9X0Z7 | - |
- |
4.4.1.13 | Thermotoga maritima DSM 3109 | Q9X0Z7 | - |
- |
4.4.1.13 | Thermotoga maritima JCM 10099 | Q9X0Z7 | - |
- |
4.4.1.13 | Wolbachia pipientis | Q73GL9 | endosymbiont of Drosophila melanogaster | - |
4.4.1.13 | Wolbachia pipientis wMel | Q73GL9 | endosymbiont of Drosophila melanogaster | - |
5.1.1.1 | Candidatus Pelagibacter ubique | Q4FME3 | - |
- |
5.1.1.1 | Candidatus Pelagibacter ubique HTCC1062 | Q4FME3 | - |
- |
5.1.1.1 | Escherichia coli | P06721 | - |
- |
5.1.1.1 | Thermotoga maritima | Q9X0Z7 | - |
- |
5.1.1.1 | Thermotoga maritima ATCC 43589 | Q9X0Z7 | - |
- |
5.1.1.1 | Thermotoga maritima DSM 3109 | Q9X0Z7 | - |
- |
5.1.1.1 | Thermotoga maritima JCM 10099 | Q9X0Z7 | - |
- |
5.1.1.1 | Wolbachia pipientis | Q73GL9 | endosymbiont of Drosophila melanogaster | - |
5.1.1.1 | Wolbachia pipientis wMel | Q73GL9 | endosymbiont of Drosophila melanogaster | - |
5.1.1.3 | Thermotoga maritima | Q9X0Z7 | - |
- |
5.1.1.3 | Thermotoga maritima ATCC 43589 | Q9X0Z7 | - |
- |
5.1.1.3 | Thermotoga maritima DSM 3109 | Q9X0Z7 | - |
- |
5.1.1.3 | Thermotoga maritima JCM 10099 | Q9X0Z7 | - |
- |
5.1.1.3 | Wolbachia pipientis | Q73GL9 | endosymbiont of Drosophila melanogaster | - |
5.1.1.3 | Wolbachia pipientis wMel | Q73GL9 | endosymbiont of Drosophila melanogaster | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.4.1.13 | cystathionine + H2O | - |
Escherichia coli | L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | - |
Candidatus Pelagibacter ubique | L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | - |
Wolbachia pipientis | L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | - |
Thermotoga maritima | L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | cystathionine + H2O | - |
Candidatus Pelagibacter ubique HTCC1062 | L-homocysteine + pyruvate + NH3 | - |
? | |
4.4.1.13 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Wolbachia pipientis | ? | - |
- |
|
4.4.1.13 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Thermotoga maritima | ? | - |
- |
|
4.4.1.13 | additional information | no activity with O-acetylhomoserine or O-succinylhomoserine plus L-cysteine, the cystathionine gamma-synthase (metB, EC 2.5.1.48) activity of the enzyme is negligible | Thermotoga maritima | ? | - |
- |
|
4.4.1.13 | additional information | the Escherichia coli cystathionine beta-lyase (CBL) also shows a promiscuous alanine racemase (ALR) activity (cf. EC 5.1.1.1). ALR catalyzes the interconversion of L-alanine and D-alanine | Escherichia coli | ? | - |
- |
|
4.4.1.13 | additional information | the GLR (EC 5.1.1.3) activity of wMelCBL is very weak: approximately 3fold less efficient than cystathionine beta-elimination (EC 4.4.1.13) and 28fold less efficient than alanine racemization (EC 5.1.1.1) | Wolbachia pipientis | ? | - |
- |
|
4.4.1.13 | additional information | the Pelagibacter ubique cystathionine beta-lyase (CBL) also shows a promiscuous alanine racemase (ALR) activity (cf. EC 5.1.1.1). ALR catalyzes the interconversion of L-alanine and D-alanine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity | Candidatus Pelagibacter ubique | ? | - |
- |
|
4.4.1.13 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Wolbachia pipientis wMel | ? | - |
- |
|
4.4.1.13 | additional information | the Pelagibacter ubique cystathionine beta-lyase (CBL) also shows a promiscuous alanine racemase (ALR) activity (cf. EC 5.1.1.1). ALR catalyzes the interconversion of L-alanine and D-alanine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity | Candidatus Pelagibacter ubique HTCC1062 | ? | - |
- |
|
5.1.1.1 | L-alanine | - |
Escherichia coli | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Candidatus Pelagibacter ubique | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Wolbachia pipientis | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Thermotoga maritima | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Wolbachia pipientis wMel | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Candidatus Pelagibacter ubique HTCC1062 | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Thermotoga maritima DSM 3109 | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Thermotoga maritima ATCC 43589 | D-alanine | - |
r | |
5.1.1.1 | L-alanine | - |
Thermotoga maritima JCM 10099 | D-alanine | - |
r | |
5.1.1.1 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Wolbachia pipientis | ? | - |
- |
|
5.1.1.1 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima | ? | - |
- |
|
5.1.1.1 | additional information | the Escherichia coli cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine | Escherichia coli | ? | - |
- |
|
5.1.1.1 | additional information | the Pelagibacter ubique cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity | Candidatus Pelagibacter ubique | ? | - |
- |
|
5.1.1.1 | additional information | TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1) | Thermotoga maritima | ? | - |
- |
|
5.1.1.1 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Wolbachia pipientis wMel | ? | - |
- |
|
5.1.1.1 | additional information | the Pelagibacter ubique cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity | Candidatus Pelagibacter ubique HTCC1062 | ? | - |
- |
|
5.1.1.1 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima DSM 3109 | ? | - |
- |
|
5.1.1.1 | additional information | TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1) | Thermotoga maritima DSM 3109 | ? | - |
- |
|
5.1.1.1 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima ATCC 43589 | ? | - |
- |
|
5.1.1.1 | additional information | TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1) | Thermotoga maritima ATCC 43589 | ? | - |
- |
|
5.1.1.1 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima JCM 10099 | ? | - |
- |
|
5.1.1.1 | additional information | TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1) | Thermotoga maritima JCM 10099 | ? | - |
- |
|
5.1.1.3 | L-glutamate | - |
Wolbachia pipientis | D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | - |
Thermotoga maritima | D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | - |
Wolbachia pipientis wMel | D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | - |
Thermotoga maritima DSM 3109 | D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | - |
Thermotoga maritima ATCC 43589 | D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | - |
Thermotoga maritima JCM 10099 | D-glutamate | - |
r | |
5.1.1.3 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Wolbachia pipientis | ? | - |
- |
|
5.1.1.3 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima | ? | - |
- |
|
5.1.1.3 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Wolbachia pipientis wMel | ? | - |
- |
|
5.1.1.3 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima DSM 3109 | ? | - |
- |
|
5.1.1.3 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima ATCC 43589 | ? | - |
- |
|
5.1.1.3 | additional information | the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria | Thermotoga maritima JCM 10099 | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.4.1.13 | dimer | the Escherichia coli ALR dimer (PDB entry 2RJG) adopts a fold type III | Escherichia coli |
4.4.1.13 | tetramer | the Escherichia coli CBL tetramer (PDB entry 1CL1) adopts a fold type I | Escherichia coli |
5.1.1.1 | dimer | the Escherichia coli ALR dimer (PDB entry 2RJG) adopts a fold type III | Escherichia coli |
5.1.1.1 | tetramer | the Escherichia coli CBL tetramer (PDB entry 1CL1) adopts fold type I | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.4.1.13 | AAR | - |
Wolbachia pipientis |
4.4.1.13 | AAR | - |
Thermotoga maritima |
4.4.1.13 | CBL | - |
Escherichia coli |
4.4.1.13 | CBL | - |
Candidatus Pelagibacter ubique |
4.4.1.13 | CBL | - |
Wolbachia pipientis |
4.4.1.13 | CBL | - |
Thermotoga maritima |
4.4.1.13 | CBL/ALR | - |
Escherichia coli |
4.4.1.13 | CBL/ALR | - |
Candidatus Pelagibacter ubique |
4.4.1.13 | CBL/ALR | - |
Wolbachia pipientis |
4.4.1.13 | CBL/ALR | - |
Thermotoga maritima |
4.4.1.13 | cystathionine beta-lyase | - |
Escherichia coli |
4.4.1.13 | cystathionine beta-lyase | - |
Candidatus Pelagibacter ubique |
4.4.1.13 | cystathionine beta-lyase | - |
Wolbachia pipientis |
4.4.1.13 | cystathionine beta-lyase | - |
Thermotoga maritima |
4.4.1.13 | EcCBL | - |
Escherichia coli |
4.4.1.13 | MetC | - |
Escherichia coli |
4.4.1.13 | MetC | - |
Candidatus Pelagibacter ubique |
4.4.1.13 | MetC | - |
Wolbachia pipientis |
4.4.1.13 | MetC | - |
Thermotoga maritima |
4.4.1.13 | More | see also EC 5.1.1.1 | Escherichia coli |
4.4.1.13 | More | see also EC 5.1.1.1 | Candidatus Pelagibacter ubique |
4.4.1.13 | More | see also EC 5.1.1.1 and EC 5.1.1.3 | Wolbachia pipientis |
4.4.1.13 | More | see also EC 5.1.1.1 and EC 5.1.1.3 | Thermotoga maritima |
4.4.1.13 | TmCBL | - |
Thermotoga maritima |
4.4.1.13 | wMelCBL | - |
Wolbachia pipientis |
5.1.1.1 | AAR | - |
Wolbachia pipientis |
5.1.1.1 | AAR | - |
Thermotoga maritima |
5.1.1.1 | ALR | - |
Escherichia coli |
5.1.1.1 | ALR | - |
Candidatus Pelagibacter ubique |
5.1.1.1 | ALR | - |
Thermotoga maritima |
5.1.1.1 | ARL | - |
Wolbachia pipientis |
5.1.1.1 | CBL/ALR | - |
Escherichia coli |
5.1.1.1 | CBL/ALR | - |
Candidatus Pelagibacter ubique |
5.1.1.1 | CBL/ALR | - |
Wolbachia pipientis |
5.1.1.1 | CBL/ALR | - |
Thermotoga maritima |
5.1.1.1 | cystathionine beta-lyase | - |
Escherichia coli |
5.1.1.1 | cystathionine beta-lyase | - |
Candidatus Pelagibacter ubique |
5.1.1.1 | cystathionine beta-lyase | - |
Wolbachia pipientis |
5.1.1.1 | cystathionine beta-lyase | - |
Thermotoga maritima |
5.1.1.1 | EcCBL | - |
Escherichia coli |
5.1.1.1 | MetC | - |
Escherichia coli |
5.1.1.1 | MetC | - |
Candidatus Pelagibacter ubique |
5.1.1.1 | MetC | - |
Wolbachia pipientis |
5.1.1.1 | MetC | - |
Thermotoga maritima |
5.1.1.1 | More | see also EC 4.4.1.13 | Escherichia coli |
5.1.1.1 | More | see also EC 4.4.1.13 | Candidatus Pelagibacter ubique |
5.1.1.1 | More | see also EC 4.4.1.13 and EC 5.1.1.3 | Wolbachia pipientis |
5.1.1.1 | More | see also EC 4.4.1.13 and EC 5.1.1.3 | Thermotoga maritima |
5.1.1.1 | TmCBL | - |
Thermotoga maritima |
5.1.1.1 | wMelCBL | - |
Wolbachia pipientis |
5.1.1.3 | AAR | - |
Wolbachia pipientis |
5.1.1.3 | AAR | - |
Thermotoga maritima |
5.1.1.3 | CBL/ALR | - |
Wolbachia pipientis |
5.1.1.3 | CBL/ALR | - |
Thermotoga maritima |
5.1.1.3 | cystathionine beta-lyase | - |
Wolbachia pipientis |
5.1.1.3 | cystathionine beta-lyase | - |
Thermotoga maritima |
5.1.1.3 | GLR | - |
Thermotoga maritima |
5.1.1.3 | GRL | - |
Wolbachia pipientis |
5.1.1.3 | MetC | - |
Wolbachia pipientis |
5.1.1.3 | MetC | - |
Thermotoga maritima |
5.1.1.3 | More | see also EC 4.4.1.13 and EC 5.1.1.1 | Wolbachia pipientis |
5.1.1.3 | More | see also EC 4.4.1.13 and EC 5.1.1.1 | Thermotoga maritima |
5.1.1.3 | TmCBL | - |
Thermotoga maritima |
5.1.1.3 | wMelCBL | - |
Wolbachia pipientis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.4.1.13 | 37 | - |
assay at | Candidatus Pelagibacter ubique |
4.4.1.13 | 37 | - |
assay at | Wolbachia pipientis |
4.4.1.13 | 70 | - |
- |
Thermotoga maritima |
5.1.1.1 | 37 | - |
assay at | Candidatus Pelagibacter ubique |
5.1.1.1 | 37 | - |
assay at | Wolbachia pipientis |
5.1.1.1 | 70 | - |
- |
Thermotoga maritima |
5.1.1.3 | 37 | - |
assay at | Wolbachia pipientis |
5.1.1.3 | 70 | - |
- |
Thermotoga maritima |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.1.3 | 35 | 90 | activity range, profile overview | Thermotoga maritima |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.4.1.13 | 0.0011 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
4.4.1.13 | 1 | - |
cystathionine | recombinant MBP-tagged enzyme, pH 8.0, 37°C | Candidatus Pelagibacter ubique | |
4.4.1.13 | 2.3 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer | Thermotoga maritima | |
4.4.1.13 | 3.3 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
4.4.1.13 | 9.2 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 0.0024 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 0.0065 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 0.022 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer | Thermotoga maritima | |
5.1.1.1 | 0.15 | - |
L-alanine | recombinant MBP-tagged enzyme, pH 8.0, 37°C | Candidatus Pelagibacter ubique | |
5.1.1.1 | 2.3 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
5.1.1.3 | 0.017 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
5.1.1.3 | 0.024 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
5.1.1.3 | 1 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.4.1.13 | 8 | - |
assay at | Candidatus Pelagibacter ubique |
4.4.1.13 | 8 | - |
assay at | Wolbachia pipientis |
4.4.1.13 | 8 | - |
assay at | Thermotoga maritima |
5.1.1.1 | 8 | - |
assay at | Candidatus Pelagibacter ubique |
5.1.1.1 | 8 | - |
assay at | Wolbachia pipientis |
5.1.1.1 | 8 | - |
assay at | Thermotoga maritima |
5.1.1.3 | 8 | - |
assay at | Wolbachia pipientis |
5.1.1.3 | 8 | - |
assay at | Thermotoga maritima |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.4.1.13 | pyridoxal 5'-phosphate | - |
Escherichia coli | |
4.4.1.13 | pyridoxal 5'-phosphate | - |
Candidatus Pelagibacter ubique | |
4.4.1.13 | pyridoxal 5'-phosphate | - |
Wolbachia pipientis | |
4.4.1.13 | pyridoxal 5'-phosphate | - |
Thermotoga maritima | |
5.1.1.1 | pyridoxal 5'-phosphate | - |
Escherichia coli | |
5.1.1.1 | pyridoxal 5'-phosphate | - |
Candidatus Pelagibacter ubique | |
5.1.1.1 | pyridoxal 5'-phosphate | - |
Wolbachia pipientis | |
5.1.1.1 | pyridoxal 5'-phosphate | - |
Thermotoga maritima | |
5.1.1.3 | pyridoxal 5'-phosphate | - |
Wolbachia pipientis | |
5.1.1.3 | pyridoxal 5'-phosphate | - |
Thermotoga maritima |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.4.1.13 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL | Escherichia coli |
4.4.1.13 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL | Candidatus Pelagibacter ubique |
4.4.1.13 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL | Wolbachia pipientis |
4.4.1.13 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL | Thermotoga maritima |
4.4.1.13 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Escherichia coli |
4.4.1.13 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Candidatus Pelagibacter ubique |
4.4.1.13 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Wolbachia pipientis |
4.4.1.13 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Thermotoga maritima |
4.4.1.13 | additional information | comparisons of structure and function of CBL and ALR, overview | Escherichia coli |
5.1.1.1 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining | Escherichia coli |
5.1.1.1 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining | Candidatus Pelagibacter ubique |
5.1.1.1 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining | Wolbachia pipientis |
5.1.1.1 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining | Thermotoga maritima |
5.1.1.1 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13) which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Candidatus Pelagibacter ubique |
5.1.1.1 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Escherichia coli |
5.1.1.1 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Wolbachia pipientis |
5.1.1.1 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Thermotoga maritima |
5.1.1.1 | additional information | comparisons of structure and function of CBL and ALR, overview | Escherichia coli |
5.1.1.3 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining | Wolbachia pipientis |
5.1.1.3 | evolution | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining | Thermotoga maritima |
5.1.1.3 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Wolbachia pipientis |
5.1.1.3 | metabolism | several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria | Thermotoga maritima |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.4.1.13 | 0.055 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
4.4.1.13 | 0.476 | - |
cystathionine | recombinant MBP-tagged enzyme, pH 8.0, 37°C | Candidatus Pelagibacter ubique | |
4.4.1.13 | 4.71 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
4.4.1.13 | 5.75 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer | Thermotoga maritima | |
4.4.1.13 | 7.08 | - |
cystathionine | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 0.00079 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 0.0052 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer | Thermotoga maritima | |
5.1.1.1 | 0.0063 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima | |
5.1.1.1 | 0.0125 | - |
L-alanine | recombinant MBP-tagged enzyme, pH 8.0, 37°C | Candidatus Pelagibacter ubique | |
5.1.1.1 | 0.605 | - |
L-alanine | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
5.1.1.3 | 0.021 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 37°C | Wolbachia pipientis | |
5.1.1.3 | 0.092 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer | Thermotoga maritima | |
5.1.1.3 | 0.71 | - |
L-glutamate | recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer | Thermotoga maritima |