PROSITE documentation PDOC00335 [for PROSITE entry PS01216]

ATP-citrate lyase / succinyl-CoA ligases signatures





Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

SUCCINYL_COA_LIG_1, PS01216; ATP-citrate lyase / succinyl-CoA ligases family signature 1  (PATTERN)

SUCCINYL_COA_LIG_2, PS00399; ATP-citrate lyase / succinyl-CoA ligases family active site  (PATTERN)

SUCCINYL_COA_LIG_3, PS01217; ATP-citrate lyase / succinyl-CoA ligases family signature 3  (PATTERN)


References

1AuthorsElshourbagy 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.
TitleCloning and expression of a human ATP-citrate lyase cDNA.
SourceEur. J. Biochem. 204:491-499(1992).
PubMed ID1371749

2AuthorsBailey D.L., Wolodko W.T., Bridger W.A.
TitleCloning, characterization, and expression of the beta subunit of pig heart succinyl-CoA synthetase.
SourceProtein Sci. 2:1255-1262(1993).
PubMed ID8401211

3AuthorsBuck D., Spencer M.E., Guest J.R.
TitlePrimary structure of the succinyl-CoA synthetase of Escherichia coli.
SourceBiochemistry 24:6245-6252(1985).
PubMed ID3002435

4AuthorsChistoserdova L.V., Lidstrom M.E.
TitleGenetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB.
SourceJ. Bacteriol. 176:7398-7404(1994).
PubMed ID7961516



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)