D
IPR020617

Thiolase, C-terminal

InterPro entry
Short nameThiolase_C
Overlapping
homologous
superfamilies
 
Thiolase-like (IPR016039)

Description

This entry represents the C-terminal domain of thiolases and related proteins.

Two different types of thiolase
[1, 2, 3]
are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase (
2.3.1.9
) and 3-ketoacyl-CoA thiolase (
2.3.1.16
). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-oxidation. Acetoacetyl-CoA thiolase (also called thiolase II) is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or steroid biogenesis.

In eukaryotes, there are two forms of 3-ketoacyl-CoA thiolase: one located in the mitochondrion and the other in peroxisomes.

There are two conserved cysteine residues important for thiolase activity. The first located in the N-terminal section of the enzymes is involved in the formation of an acyl-enzyme intermediate; the second located at the C-terminal extremity is the active site base involved in deprotonation in the condensation reaction.

Mammalian nonspecific lipid-transfer protein (nsL-TP) (also known as sterol carrier protein 2) is a protein which seems to exist in two different forms: a 14 Kd protein (SCP-2) and a larger 58 Kd protein (SCP-x). The former is found in the cytoplasm or the mitochondria and is involved in lipid transport; the latter is found in peroxisomes. The C-terminal part of SCP-x is identical to SCP-2 while the N-terminal portion is evolutionary related to thiolases
[1]
.

References

1.Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx. Baker ME, Billheimer JT, Strauss JF 3rd. DNA Cell Biol. 10, 695-8, (1991). PMID: 1755959

2.Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon. Yang SY, Yang XY, Healy-Louie G, Schulz H, Elzinga M. J. Biol. Chem. 265, 10424-9, (1990). View articlePMID: 2191949

3.Phylogenetic analysis of the thiolase family. Implications for the evolutionary origin of peroxisomes. Igual JC, Gonzalez-Bosch C, Dopazo J, Perez-Ortin JE. J. Mol. Evol. 35, 147-55, (1992). View articlePMID: 1354266

GO terms

biological process

  • None

cellular component

  • None

Cross References

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