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1 Publications
First Author | Title | Year | Journal | Volume | Pages |
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Antranikian G | Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation. | 1985 | Eur J Biochem | 153 | 413-20 |
Name | Citrate lyase ligase, C-terminal | Short Name | Citrate_lyase_ligase_C |
Type | Domain | Description | [Citrate (pro-3S)-lyase]ligase (), also known as citrate lyase ligase, is responsible for acetylation of the prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase. It converts the inactive thiol form of the enzyme to the active form. In Clostridium sphenoides, citrate lyase ligase actively degrades citrate. In Clostridium sporosphaeroidesand Lactococcus lactis, however, the enzyme is under stringent regulatory control. The enzyme's activity in anaerobic bacteria is modulated by phosphorylation and dephosphorylation [].The proteins in this entry represent the C-terminal domain of citrate lyase ligase. |
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First Author | Title | Year | Journal | Volume | Pages |
---|---|---|---|---|---|
Antranikian G | Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation. | 1985 | Eur J Biochem | 153 | 413-20 |
To cite PlanMine, please refer to the following publication:Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C. |