EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.87 | dithioerythritol | formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme | Klebsiella pneumoniae | |
4.1.1.87 | hydroxylamine | formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme | Klebsiella pneumoniae | |
4.1.1.88 | dithioerythritol | formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme | Klebsiella pneumoniae | |
4.1.1.88 | hydroxylamine | formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme | Klebsiella pneumoniae |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.1.87 | 12000 | - |
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
4.1.1.87 | 30000 | - |
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
4.1.1.87 | 65000 | - |
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
4.1.1.87 | 142000 | - |
gel filtration | Klebsiella pneumoniae |
4.1.1.88 | 12000 | - |
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
4.1.1.88 | 30000 | - |
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
4.1.1.88 | 65000 | - |
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
4.1.1.88 | 142000 | - |
gel filtration | Klebsiella pneumoniae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.87 | Klebsiella pneumoniae | - |
- |
- |
4.1.1.88 | Klebsiella pneumoniae | - |
- |
- |
6.2.1.35 | Klebsiella pneumoniae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.87 | - |
Klebsiella pneumoniae |
4.1.1.88 | - |
Klebsiella pneumoniae |
6.2.1.35 | during purification of the malonate decarboxylase complex, the ligase is separated from the decarboxylase by treatment with 1.5 M ammonium sulfate after the TSK-DEAE column | Klebsiella pneumoniae |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.1.1.87 | a malonyl-[acyl-carrier protein] = an acetyl-[acyl-carrier protein] + CO2 | malonate decarboxylation proceeds in two steps: the acetyl residue on the acyl carrier protein is first replaced by a malonyl residue which subsequently undergoes decarboxylation thereby regenerating the acetyl-S-acyl carrier protein | Klebsiella pneumoniae | |
4.1.1.88 | malonate + H+ + Na+[side 1] = acetate + CO2 + Na+[side 2] | malonate decarboxylation proceeds in two steps: the acetyl residue on the acyl carrier protein is first replaced by a malonyl residue which subsequently undergoes decarboxylation thereby regenerating the acetyl-S-acyl carrier protein | Klebsiella pneumoniae |
EC Number | Renatured (Comment) | Organism |
---|---|---|
4.1.1.87 | reacylation of the catalytically inactive SH-enzyme to form the catalytically active acetyl-S-enzyme can be achieved with acetic anhydride or more efficiently with malonyl-CoA | Klebsiella pneumoniae |
4.1.1.88 | reacylation of the catalytically inactive SH-enzyme to form the catalytically active acetyl-S-enzyme can be achieved with acetic anhydride or more efficiently with malonyl-CoA | Klebsiella pneumoniae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.35 | additional information | catalytic mechanism of malonate decarboxylase and involvement of ACP-SH acetate:ligase | Klebsiella pneumoniae | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.87 | More | presence of two forms of the enzyme: a catalytically inactive SH-enzyme and the catalytically active acetyl-S-enzyme which is formed by post-translational acetylation of the SH-enzyme with ATP, acetate and a specific ligase. the delta subunit is the acyl carrier protein of the enzyme complex | Klebsiella pneumoniae |
4.1.1.87 | tetramer | 1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
4.1.1.88 | More | presence of two forms of the enzyme: a catalytically inactive SH-enzyme and the catalytically active acetyl-S-enzyme which is formed by post-translational acetylation of the SH-enzyme with ATP, acetate and a specific ligase. the delta subunit is the acyl carrier protein of the enzyme complex | Klebsiella pneumoniae |
4.1.1.88 | tetramer | 1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE | Klebsiella pneumoniae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.87 | additional information | the binding site for the acyl residues on the acyl carrier protein is 2'-(5''-phosphoribosyl)-3'-dephospho-CoA | Klebsiella pneumoniae |