S
IPR033847

ATP-citrate lyase/succinyl-CoA ligase, conserved site

InterPro entry
Short nameCitrt_syn/SCS-alpha_CS

Description

There are four different enzymes that 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 (
4.1.3.8
)
[4]
, the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues, catalyses 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) (
6.2.1.4
)
[2]
is a mitochondrial enzyme that catalyses 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 alpha and a beta subunits.
 * Succinyl-CoA ligase (ADP-forming) (
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 alpha and two beta subunits.
 * Malate-CoA ligase (
6.2.1.9
) (malyl-CoA synthetase)
[1]
, 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.


This entry corresponds to a glycine-rich conserved region, located in the second half of ATP citrate lyase and in the alpha subunits of succinyl-CoA ligases and malate-CoA ligase.

References

1.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. Chistoserdova LV, Lidstrom ME. J. Bacteriol. 176, 7398-404, (1994). View articlePMID: 7961516

2.Cloning, characterization, and expression of the beta subunit of pig heart succinyl-CoA synthetase. Bailey DL, Wolodko WT, Bridger WA. Protein Sci. 2, 1255-62, (1993). View articlePMID: 8401211

3.Primary structure of the succinyl-CoA synthetase of Escherichia coli. Buck D, Spencer ME, Guest JR. Biochemistry 24, 6245-52, (1985). View articlePMID: 3002435

4.Cloning and expression of a human ATP-citrate lyase cDNA. Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS. Eur. J. Biochem. 204, 491-9, (1992). View articlePMID: 1371749

Cross References

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