Lyases are one of the major classifications of enzymes.  These enzymes are responsible for breaking double bonds through the addition of water, ammonia, or carbon dioxide.  Lyases can also form double bonds by the removal of these products from the substrate.  Lyases are found in both prokaryotic and eukaryotic organisms, and in an equally diverse range of biological pathways.  This page will focus on three different examples: Fructose-1,6-bisphosphate aldolase, isolated from the malaria parasite Plasmodium falciparum; Pectate lyase, isolated from Bacillus subtilis; and rat type II adenylyl cyclase C2 domain.  All three of these structures have been determined by X-ray crystallography and will be discussed in further detail.

Fructose-1,6-bisphosphate aldolase isolated from Human Malaria Parasite Plasmodium falciparum

Pectate Lyase isolated from Bacillus subilis in complex with calium

Type II Adenylyl Cyclase C2 Domain isolated from a rat in complex with forskolin

Web Resources
Pub Med

Protein data bank

ExPASy Proteomics Server

NCBI (National Center for Biotechnology Information)

EBI (European Bioinformatics Institute)

CATH (Class, Architecture, Topology, Homology - Protein Structural Classification)

SCOP (Structural Classification of Proteins)

ALIGN (Pairwise sequence alignment)

Introduction to Lyases
[Home] [Introduction] [Fructose-1,6-Bisphosphate Aldolase] [Pectate Lyase]

[Type II Adenylyl Cyclase] [References] [Conclusion]