EC Number | Cloned (Comment) | Organism |
---|---|---|
2.6.1.62 | - |
Mycobacterium tuberculosis |
2.6.1.105 | - |
Bacillus subtilis |
6.3.3.3 | expression in Escherichia coli | Mycobacterium tuberculosis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.6.1.62 | to 2.2 A resolution, by molecular replacement, and superimposition of the structures bound either to the S-adenosyl-L-methionine analog sinefungin or to 7-oxo-8-aminopelargonic acid. Comparison to structure of the Bacillus subtilis enzyme, EC 2.5.1.105 | Mycobacterium tuberculosis |
2.6.1.105 | to 2.2 A resolution, by molecular replacement. The overall structure is similar to its Mycobacterium tubrculosis and Escherichia coli counterparts, EC 2.6.1.62. Unlike the counterparts, a large part of the active site, i.e. Lys143-Glu172, is completely disordered in both chains. The substrate stabilizes the loop region of the Bacillus subtilis active site | Bacillus subtilis |
6.3.3.3 | in complexes with the substrate 7,8-diaminopelargonic acid or ADP and the product dethiobiotin, up to 1.85 A resolution. | Mycobacterium tuberculosis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.6.1.62 | 0.45 | - |
S-adenosyl-L-methionine | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis | |
2.6.1.62 | 0.7 | - |
sinefungin | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis | |
6.3.3.3 | 0.002 | - |
7,8-diaminononanoate | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis | |
6.3.3.3 | 0.029 | - |
ATP | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.6.1.62 | Mycobacterium tuberculosis | P9WQ80 | - |
- |
2.6.1.62 | Mycobacterium tuberculosis CDC 1551 | P9WQ80 | - |
- |
2.6.1.105 | Bacillus subtilis | P53555 | - |
- |
2.6.1.105 | Bacillus subtilis 168 | P53555 | - |
- |
6.3.3.3 | Mycobacterium tuberculosis | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.3.3.3 | ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin | enzyme reaction involves three steps: carbamylation of theN7 position of 7,8-diaminononanoate, formation of a carbamate-phosphoric anhydride intermediate, and, closure of the ureido ring to form dethiobiotin and release of the inorganic phosphate | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate | - |
Mycobacterium tuberculosis | S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate | - |
? | |
2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate | - |
Mycobacterium tuberculosis CDC 1551 | S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate | - |
? | |
2.6.1.62 | S-adenosyl-L-methionine + sinefungin | - |
Mycobacterium tuberculosis | S-adenosyl-4-methylthio-2-oxobutanoate + ? | - |
? | |
2.6.1.62 | S-adenosyl-L-methionine + sinefungin | - |
Mycobacterium tuberculosis CDC 1551 | S-adenosyl-4-methylthio-2-oxobutanoate + ? | - |
? | |
2.6.1.105 | additional information | presence of substrate stabilizes the loop region of the active site | Bacillus subtilis | ? | - |
? | |
2.6.1.105 | additional information | presence of substrate stabilizes the loop region of the active site | Bacillus subtilis 168 | ? | - |
? | |
6.3.3.3 | ATP + 7,8-diaminononanoate + CO2 | - |
Mycobacterium tuberculosis | ADP + phosphate + dethiobiotin | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.6.1.105 | bioA | - |
Bacillus subtilis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.6.1.62 | 0.009 | - |
sinefungin | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis | |
2.6.1.62 | 0.012 | - |
S-adenosyl-L-methionine | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.62 | S-adenosyl-L-methionine | - |
Mycobacterium tuberculosis |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.6.1.62 | 0.013 | - |
sinefungin | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis | |
2.6.1.62 | 0.03 | - |
S-adenosyl-L-methionine | pH 7.5, temperature not specified in the publication | Mycobacterium tuberculosis |