---
pmid: '1320004'
title: A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster
  (mutation killer of prune) affects stability but not catalytic efficiency of the
  enzyme.
authors:
- Lascu I
- Chaffotte A
- Limbourg-Bouchon B
- Véron M
journal: J Biol Chem
year: '1992'
full_text_available: false
pubmed_publication_types:
- Journal Article
- Research Support, Non-U.S. Gov't
publication_type: PRIMARY_RESEARCH
---

# A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster (mutation killer of prune) affects stability but not catalytic efficiency of the enzyme.
**Authors:** Lascu I, Chaffotte A, Limbourg-Bouchon B, Véron M
**Journal:** J Biol Chem (1992)

## Abstract

1. J Biol Chem. 1992 Jun 25;267(18):12775-81.

A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila
melanogaster (mutation killer of prune) affects stability but not catalytic
efficiency of the enzyme.

Lascu I(1), Chaffotte A, Limbourg-Bouchon B, Véron M.

Author information:
(1)Unité de Biochimie Cellulaire (URA 1129), Institut Pasteur, Paris, France.

Nucleoside diphosphate kinase of Drosophila, recently identified as the product
of the awd gene, is essential for larval development. The conditional lethal
mutation Killer of prune maps to the same gene. We purified the nucleoside
diphosphate kinases from wild-type and mutant larvae by a simple procedure
involving affinity chromatography on blue Sepharose. Both proteins are purified
as hexamers in their native state. The mutant protein, which carries a serine
instead of proline at position 97, has structural properties and catalytic
efficiency that are very similar to the wild-type protein. However, the mutant
protein has a much lower stability to denaturation by heat and urea. Following
dilution of urea with buffer the urea-denaturated mutant nucleoside diphosphate
kinase accumulates as folded monomers and cannot recover its quaternary
structure and enzymatic activity. In contrast, the wild-type enzyme recovers
hexameric structure and activity. This suggests that the mutation affects the
folding/assembly pathway without affecting the function of the mature protein
once folded and assembled into the mature hexameric structure.

PMID: 1320004 [Indexed for MEDLINE]