Domain relationships in thiamine diphosphate-dependent enzymes.
Three-dimensional structures have been determined for 13 different enzymes that use thiamine diphosphate (ThDP) as a cofactor. These enzymes fall into five families, where members within a family have similar structures. In different families, there are similarities between some domains that clearly point to a common ancestor for all of these enzymes. Where the enzyme structures differ, evolutionary relationships between families can be discerned. Here, I present an analysis of these families and propose an evolutionary pathway to explain the diversity of structures that are now known.
Duggleby
Ronald G
RG
School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Queensland 4072, Australia. ronald.duggleby@uq.edu.au
D002244:Carbon / Q000737:chemistry; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D017434:Protein Structure, Tertiary; D013835:Thiamine Pyrophosphate / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology*
D002244:Carbon; D002262:Carboxy-Lyases; D013835:Thiamine Pyrophosphate