H
IPR016143

Citrate synthase-like, small alpha subdomain

InterPro entry
Short nameCitrate_synth-like_sm_a-sub
Overlapping entries
 
Citrate synthase (IPR002020)

Description

This entry represents the small α-helical domain from type I and II citrate synthase enzymes, as well as a homolgous domain found in the related enzyme ATP citrate synthase. ATP citrate synthase (
2.3.3.8
) (also known as ATP citrate lyase) catalyses the MgATP-dependent, CoA-dependent cleavage of citrate into oxaloacetate and acetyl-CoA, a key step in the reductive tricarboxylic acid pathway of CO2 assimilation used by a variety of autotrophic bacteria and archaea to fix carbon dioxide
[1]
. ATP citrate synthase is composed of two distinct subunits. In eukaryotes, ATP citrate synthase is a homotetramer of a single large polypeptide, and is used to produce cytosolic acetyl-CoA from mitochondrial-produced citrate
[2]
.

Citrate synthase
2.3.3.1
is a member of a small family of enzymes that can directly form a carbon-carbon bond without the presence of metal ion cofactors. It catalyses the first reaction in the Krebs' cycle, namely the conversion of oxaloacetate and acetyl-coenzyme A into citrate and coenzyme A. This reaction is important for energy generation and for carbon assimilation. The reaction proceeds via a non-covalently bound citryl-coenzyme A intermediate in a 2-step process (aldol-Claisen condensation followed by the hydrolysis of citryl-CoA).

References

1.Both subunits of ATP-citrate lyase from Chlorobium tepidum contribute to catalytic activity. Kim W, Tabita FR. J. Bacteriol. 188, 6544-52, (2006). View articlePMID: 16952946

2.ATP citrate lyase is an important component of cell growth and transformation. Bauer DE, Hatzivassiliou G, Zhao F, Andreadis C, Thompson CB. Oncogene 24, 6314-22, (2005). View articlePMID: 16007201

Further reading

3. Investigating the accessibility of the closed domain conformation of citrate synthase using essential dynamics sampling. Daidone I, Roccatano D, Hayward S. J. Mol. Biol. 339, 515-25, (2004). View articlePMID: 15147839

4. Structure of a NADH-insensitive hexameric citrate synthase that resists acid inactivation. Francois JA, Starks CM, Sivanuntakorn S, Jiang H, Ransome AE, Nam JW, Constantine CZ, Kappock TJ. Biochemistry 45, 13487-99, (2006). View articlePMID: 17087502

Cross References

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