Lipoylating and biotinylating enzymes contain a homologous catalytic module



Downloads per month over past year

Reche, Pedro A (2000) Lipoylating and biotinylating enzymes contain a homologous catalytic module. Protein science : a publication of the Protein Society, 9 (10). pp. 1922-9. ISSN 0961-8368

[thumbnail of 10.Reche_PS_2001.pdf]


Biotin and lipoic acid moieties are the covalently attached coenzyme cofactors of several multicomponent enzyme complexes that catalyze key metabolic reactions. Attachment of these moieties to the biotinyl- and lipoyl-dependent enzymes is post-translationally catalyzed by specific biotinylating and lipoylating protein enzymes. In Escherichia coli, two different enzymes, LplA and LipB, catalyze independent pathways for the lipoylation of the relevant enzymes, whereas only one enzyme, the BirA protein, is responsible for all the biotinylation. Counterparts of the E. coli BirA, LplA, and LipB enzymes have been previously identified in many organisms, but homology among the three families has never been reported. Computational analysis based on PSI-BLAST profiles and secondary structure predictions indicates, however, that lipoylating and biotinylating enzymes are evolutionarily related protein families containing a homologous catalytic module. Sequence conservation among the three families is very poor, but a single lysine residue is strictly conserved in all of them, which, according to the available X-ray crystal structure of the E. coli BirA protein, is expected to contribute to the binding of lipoic acid in the LplA and LipB enzymes.

Item Type:Article
Uncontrolled Keywords:Biotinyl0lipoyl protein ligase; Biotinylation0lipoylation; Database searches; Protein evolution; Secondary structure; Sequence space; Structure prediction
Subjects:Medical sciences > Biology > Evolution
Medical sciences > Biology > Molecular biology
Sciences > Computer science > Bioinformatics
ID Code:9347
Deposited On:10 Aug 2009 08:20
Last Modified:13 Dec 2018 12:48

Origin of downloads

Repository Staff Only: item control page