Secondly, candidate ligases,
carboxylases and the cognate acyltransferase domains that specifically recruit the unusual extender units will be studied in vitro for substrate specificity and for their ability to accept non-natural substrates bearing chemical functionality.
Biotin is known to play an essential role in metabolic pathways such as gluconeogenesis and fatty acid synthesis by acting as a prosthetic group for
carboxylases.
Differencial activation of recombinant human acetyl-CoA
carboxylases 1 and 2 by citrate.
In humans, biotin is a coenzyme for 4 important
carboxylases in fatty acid synthesis, branched-chain amino acid catabolism, and gluconeogenesis (4, 5).
It is an important cofactor to several enzymes, including acetyl CoA
carboxylase and other
carboxylases.
Structural similarity and functional differences between invertebrate and vertebrate
carboxylases: expression and characterization of recombinant vitamin K-dependent [beta]-glutamyl
carboxylase from Conus textile.
Biotin is a cofactor in metabolic reactions which require
carboxylases.
Given the functional similarity of mammalian vitamin K-dependent
carboxylases and the vitamin K-dependent
carboxylase from Conus textile, we hypothesized that structurally conserved regions would identify sequences critical to this common functionality.
The current study suggests the presence of an association among milk production and genetic polymorphism in the exon I region of Acetyl Coenzyme A
Carboxylase a (ACACA) in Iranian indigenous Mahabadi goat.
