EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.3.2.8 | H199A | mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates | Escherichia coli |
6.3.2.8 | K130A | mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates | Escherichia coli |
6.3.2.8 | N293A | mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates | Escherichia coli |
6.3.2.8 | N296A | mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates | Escherichia coli |
6.3.2.8 | R327A | mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.2.8 | additional information | - |
additional information | Km-value of wild-type and mutant enzymes | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.2.8 | Escherichia coli | - |
wild-type and mutant enzymes | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.3.2.8 | ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine | the binding order of the substrates can be ATP, UDP-N-acetylmuramate, and Ala | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.2.8 | ATP + UDP-N-acetylmuramate + L-Ala | - |
Escherichia coli | ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala | - |
? |