Home  |  Contact
PROSITE documentation PDOC00423

Aconitase family signatures





Description

Aconitase (aconitate hydratase) (EC 4.2.1.3) [1] is the enzyme from the tricarboxylic acid cycle that catalyzes the reversible isomerization of citrate and isocitrate. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster.

It has been shown that the aconitase family also contains the following proteins:

  • Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity.
  • 3-isopropylmalate dehydratase (EC 4.2.1.33) (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine.
  • Homoaconitase (EC 4.2.1.36) (homoaconitate hydratase), an enzyme that participates in the α-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
  • Esherichia coli protein ybhJ.

As a signature for proteins from the aconitase family we have selected two conserved regions that contain the three cysteine ligands of the 4Fe-4S cluster.

Last update:

December 2004 / Pattern and text revised.

Technical section

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

ACONITASE_1, PS00450; Aconitase family signature 1  (PATTERN)

ACONITASE_2, PS01244; Aconitase family signature 2  (PATTERN)


Reference

1AuthorsGruer M.J. Artymiuk P.J. Guest J.R.
TitleThe aconitase family: three structural variations on a common theme.
SourceTrends Biochem. Sci. 22:3-6(1997).
PubMed ID9020582



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)