Structural insights into the evolution of the pantothenate-biosynthesis pathway.
Pantothenate is synthesized in bacteria, fungi and plants, and as vitamin B5 is a dietary requirement in animals. The three-dimensional structures of the four Escherichia coli enzymes involved in the production of pantothenate have been determined. We describe the use of comparative analyses of the sequences and structures to identify distant homologues of the four enzymes in an attempt to understand the evolution of the pathway. We conclude that it is likely to have evolved via a patchwork mechanism, whereby the individual enzymes were recruited separately.
Lobley
C M C
CM
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK. carina@cryst.bioc.cam.ac.uk
Schmitzberger
F
F
Kilkenny
M L
ML
Whitney
H
H
Ottenhof
H H
HH
Chakauya
E
E
Webb
M E
ME
Birch
L M
LM
Tuck
K L
KL
Abell
C
C
Smith
A G
AG
Blundell
T L
TL
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D030562:Databases, Protein; D004926:Escherichia coli / Q000201:enzymology*; D019143:Evolution, Molecular; D019877:Hydroxymethyl and Formyl Transferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010205:Pantothenic Acid / Q000096:biosynthesis*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D010446:Peptide Fragments; D010205:Pantothenic Acid; D019877:Hydroxymethyl and Formyl Transferases; C021477:3-methyl-2-oxobutanoate hydroxymethyltransferase