# Transformylase Enzymes Dihydrofolate Reductase

> **NIH NIH R01** · PENNSYLVANIA STATE UNIVERSITY, THE · 2020 · $258,885

## 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 organization:** PENNSYLVANIA STATE UNIVERSITY, THE
- **Principal Investigator:** STEPHEN J BENKOVIC
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $258,885
- **Award type:** 5
- **Project period:** 1977-07-01 → 2021-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/9900786

## Citation

> US National Institutes of Health, RePORTER application 9900786, Transformylase Enzymes Dihydrofolate Reductase (5R01GM024129-39). Retrieved via AI Analytics 2026-05-24 from https://api.ai-analytics.org/grant/nih/9900786. Licensed CC0.

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