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| PROSITE documentation PDOC00335 [for PROSITE entry PS00399] |
ATP-citrate lyase / succinyl-CoA ligases signatures
Four different enzymes share a similar catalytic mechanism which involves the phosphorylation by ATP (or GTP) of a specific histidine residue in the active site. These enzymes are:
- ATP citrate-lyase (EC 2.3.3.8) [1], the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues, catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with the concomitant hydrolysis of ATP to ADP and phosphate. ATP-citrate lyase is a tetramer of identical subunits.
- Succinyl-CoA ligase (GDP-forming) (EC 6.2.1.4) [2] is a mitochondrial enzyme that catalyzes the substrate level phosphorylation step of the tricarboxylic acid cycle: the formation of succinyl-CoA from succinate with a concomitant hydrolysis of GTP to GDP and phosphate. This enzyme is a dimer composed of an α and a β subunits.
- Succinyl-CoA ligase (ADP-forming) (EC 6.2.1.5) [3] is a bacterial enzyme that during aerobic metabolism functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP. It can also function in the other direction for anabolic purposes. This enzyme is a tetramer composed of two α and two β subunits.
- Malate-CoA ligase (EC 6.2.1.9) (malyl-CoA synthetase) [4], is a bacterial enzyme that forms malyl-CoA from malate and CoA with the concomitant hydrolysis of ATP to ADP and phosphate. Malate-CoA ligase is composed of two different subunits.
We developed three signature patterns for these enzymes, the first corresponds to a glycine-rich conserved region, located in the second half of ATP citrate lyase and in the α subunits of succinyl-CoA ligases and malate-CoA ligase. The second pattern, which is located some 50 residues to the C-terminal of the first one, includes the active site phosphorylated histidine residue. The last pattern corresponds to a conserved region located in the first half of ATP citrate lyase and in the β subunits of succinyl-CoA ligases and malate-CoA ligase.
Last update:April 2006 / Pattern revised.
PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Elshourbagy N.A., Near J.C., Kmetz P.J., Wells T.N., Groot P.H., Saxty B.A., Hughes S.A., Franklin M., Gloger I.S. |
| Title | Cloning and expression of a human ATP-citrate lyase cDNA. | |
| Source | Eur. J. Biochem. 204:491-499(1992). | |
| PubMed ID | 1371749 |
| 2 | Authors | Bailey D.L., Wolodko W.T., Bridger W.A. |
| Title | Cloning, characterization, and expression of the beta subunit of pig heart succinyl-CoA synthetase. | |
| Source | Protein Sci. 2:1255-1262(1993). | |
| PubMed ID | 8401211 |
| 3 | Authors | Buck D., Spencer M.E., Guest J.R. |
| Title | Primary structure of the succinyl-CoA synthetase of Escherichia coli. | |
| Source | Biochemistry 24:6245-6252(1985). | |
| PubMed ID | 3002435 |
| 4 | Authors | Chistoserdova L.V., Lidstrom M.E. |
| Title | Genetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB. | |
| Source | J. Bacteriol. 176:7398-7404(1994). | |
| PubMed ID | 7961516 |
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