Volume 272, Number 48, Issue of November 28, 1997
pp. 29985-29985
MINIREVIEW PROLOGUE:
Minireview Series on Enzyme Superfamilies*
Kathleen S.
Matthews
From the Department of Biochemistry and Cell Biology, Rice
University, Houston, Texas 77005-1892
INTRODUCTION
- FOOTNOTES
INTRODUCTION 
Structural superfamilies of
proteins, encompassing an increasing number of enzymes, have been
identified. Some families share a common structural motif and similar
enzymatic activity but have varying substrate specificities. In
contrast, other families share structural motifs that catalyze quite
distinct overall reactions. In this issue, John J. Perona and Charles
S. Craik provide a perspective on the relationship between substrate
specificity and structural organization in the chymotrypsin-like serine
protease superfamily. Significant alterations in closely related
structures can derive from accommodation of differences in substrate
specificity.
In the next issue, Patricia C. Babbitt and John A. Gerlt provide an
evolutionary perspective on enzyme superfamilies in which a common
structural scaffold catalyzes distinct chemical reactions. Despite the
diversity of function in these enzymes, the basic chemistry of the
reaction, a common mechanistic strategy, underlies development of new
catalytic activities. As further insights into protein structure and
function are derived from examination of protein superfamilies,
principles that govern the relationship between structure and function
may emerge that will allow assignment of catalytic function to the
growing number of sequences with unknown roles. This arena of
investigation will continue to provide great excitement and elicit
significant interest as studies on additional protein superfamilies are
integrated.
FOOTNOTES
*
These minireviews will be reprinted in the 1997 Minireview
Compendium, which will be available in December, 1997.
Volume 272, Number 48,
Issue of November 28, 1997
pp. 29985-29985
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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