Transformylase Enzymes Dihydrofolate Reductase

NIH RePORTER · NIH · R01 · $258,885 · view on reporter.nih.gov ↗

Abstract

Project Summary/Abstract A unique level of metabolic enzyme organization within a cell is the formation of metabolons. Metabolons have been hypothesized to promote more efficient processing of metabolites through enzyme clustering to meet cellular demand. In the case of high purine demand, the enzymes involved in de novo purine biosynthesis spatially organize to form multi-enzyme clusters coined as purinosomes. Conditions that impact purine biosynthesis were shown to modulate purinosome formation suggesting that the purinosome may act as a marker for de novo purine biosynthetic pathway activation. This proposal focuses on exploring the purinosome as an example of a transient metabolon. These molecular understandings generated will provide further insights into how the cell leverages the de novo purine biosynthetic pathway under high purine demand and provides a general framework for studying metabolons.

Key facts

NIH application ID
9900786
Project number
5R01GM024129-39
Recipient
PENNSYLVANIA STATE UNIVERSITY, THE
Principal Investigator
STEPHEN J BENKOVIC
Activity code
R01
Funding institute
NIH
Fiscal year
2020
Award amount
$258,885
Award type
5
Project period
1977-07-01 → 2021-03-31