Chemical Society Reviews 2011-08-01

Vitamin B12-derivatives-enzyme cofactors and ligands of proteins and nucleic acids.

Karl Gruber, Barbara Puffer, Bernhard Kräutler

Index: Chem. Soc. Rev. 40 , 4346-4363, (2011)

Full Text: HTML

Abstract

B(12)-cofactors play important roles in the metabolism of microorganisms, animals and humans. Microorganisms are the only natural sources of B(12)-derivatives, and the latter are "vitamins" for other B(12)-requiring organisms. Some B(12)-dependent enzymes catalyze complex isomerisation reactions, such as methylmalonyl-CoA mutase. They need coenzyme B(12), an organometallic B(12)-derivative, to induce enzymatic radical reactions. Another group of widely relevant enzymes catalyzes the transfer of methyl groups, such as methionine synthase, which uses methylcobalamin as cofactor. This tutorial review covers structure and reactivity of B(12)-derivatives and structural aspects of their interactions with proteins and nucleotides, which are crucial for the efficient catalysis by the important B(12)-dependent enzymes, and for achieving and regulating uptake and transport of B(12)-derivatives.This journal is © The Royal Society of Chemistry 2011


Related Compounds

Related Articles:

Alanine Scanning Mutagenesis Identifies an Asparagine–Arginine–Lysine Triad Essential to Assembly of the Shell of the Pdu Microcompartment

2008-01-01

[J. Mol. Biol. 426(12) , 2328-45, (2014)]

Tissue vitamin concentrations are maintained constant by changing the urinary excretion rate of vitamins in rats' restricted food intake.

2014-01-01

[Biosci. Biotechnol. Biochem. 78(12) , 2102-9, (2014)]

Effect of concentrate feeder design on performance, eating and animal behavior, welfare, ruminal health, and carcass quality in Holstein bulls fed high-concentrate diets.

2015-06-01

[J. Anim. Sci. 93 , 3018-33, (2015)]

Solubilization of gliadins for use as a source of nitrogen in the selection of bacteria with gliadinase activity.

2015-02-01

[Food Chem. 168 , 439-44, (2014)]

Disease mutations in desmoplakin inhibit Cx43 membrane targeting mediated by desmoplakin-EB1 interactions.

2014-09-15

[J. Cell Biol. 206(6) , 779-97, (2014)]

More Articles...