Protein Variants | Comment | Organism |
---|---|---|
H662A | inactive | Escherichia coli |
Y477W | KM-value for ATP is 1.75fold higher than wild-type value. kcat for ATP is 4.3fold higher than wild-type value | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.36 | - |
ATP | wild-type enzyme | Escherichia coli | |
0.63 | - |
ATP | mutant enzyme Y477W | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + alpha-haemolysin/in | - |
Escherichia coli | ADP + phosphate + alpha-haemolysin/out | - |
? | |
additional information | one intact nucleotide-binding domain within a dimer is sufficient for ATP hydrolysis. One ATP-binding site of the dimer is able to function independently of the hydrolytic capability of the neighboring ATP-binding site. Sequential mechanism of ATP hydrolysis in the intact HlyB transporter | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | is the active form of the enzyme. ATP-promoted dimerization of HlyB-nucleotide binding domain might involve formation of two interconvertible forms: a readily dissociable active dimer and a more stable, reversibly inactive form of the dimer | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
haemolysin B transporter | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.021 | - |
ATP | mutant enzyme Y477W | Escherichia coli | |
0.093 | - |
ATP | wild-type enzyme | Escherichia coli |