Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochemistry. 1997 Jun 3;36(22):6709-16.

Formyl phosphate: a proposed intermediate in the reaction catalyzed by Escherichia coli PurT GAR transformylase.

Author information

1
Department of Chemistry, The Pennsylvania State University, University Park 16802, USA.

Abstract

The Escherichia coli purT encoded glycinamide ribonucleotide transformylase (GAR transformylase) serves as an alternate enzyme in the production of formyl GAR for use in de novo purine biosynthesis. This enzyme differs from the previously known purN encoded enzyme in size, sequence, and substrates; ATP and formate are required as opposed to formyl tetrahydrofolate. Kinetic studies of the wild-type PurT enzyme described here demonstrate that formyl phosphate behaves as a chemically and kinetically competent intermediate. The requirement for ATP and GAR in these reactions is consistent with previous steady-state kinetic results, which demonstrated that all substrates must be bound before catalysis. Kinetic characterization of a mutant, which releases formyl phosphate into solution, and positional isotope exchange studies also support the assignment of formyl phosphate as a plausible intermediate.

PMID:
9184151
DOI:
10.1021/bi962961p
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society
    Loading ...
    Support Center