Methenyltetrahydrofolate synthetase is a high-affinity catecholamine-binding protein. Academic Article

abstract

• Recombinant mouse 5,10-methenyltetrahydrofolate synthetase (MTHFS) was expressed in Escherichia coli and shown to co-purify with a chromophore that had a lambda(max) at 320nm. The chromophore remained bound to MTHFS during extensive dialysis, but dissociated from MTHFS when its substrate, 5-formyltetrahydrofolate, was bound. The chromophore was identified as an oxidized catecholamine by mass spectrometry and absorption spectroscopy. Purified recombinant mouse MTHFS and rabbit liver MTHFS proteins were shown to bind oxidized N-acetyldopamine (NADA) tightly. The addition of NADA to cell culture medium accelerated markedly folate turnover and decreased both folate accumulation and total cellular folate concentrations in MCF-7 cells. Expression of the MTHFS cDNA in MCF-7 cells increased the concentration of NADA required to deplete cellular folate. The results of this study are the first to identify a link between catecholamines and one-carbon metabolism and demonstrate that NADA accelerates folate turnover and impairs cellular folate accumulation in MCF-7 cells.

authors

• Stover, Patrick

published proceedings

• Arch Biochem Biophys

altmetric score

• 3

author list (cited authors)

• Anguera, M. C., & Stover, P. J.

citation count

• 5

complete list of authors

• Anguera, Montserrat C||Stover, Patrick J

publication date

• November 2006

publisher

• Elsevier  Publisher

published in

• Archives of Biochemistry and Biophysics  Journal

keywords

• Animals
• Binding Sites
• Breast Neoplasms
• Carbon-nitrogen Ligases
• Catecholamines
• Cell Line, Tumor
• Enzyme Activation
• Folic Acid
• Humans
• Mice
• Protein Binding
• Rabbits
• Substrate Specificity

PubMed Central ID

• 17055997

Digital Object Identifier (DOI)

• 10.1016/j.abb.2006.09.008

start page

• 175

end page

• 187

volume

• 455

issue

• 2

URL

• http://dx.doi.org/10.1016/j.abb.2006.09.008