Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid.
The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A. The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA).
Erskine
P T
PT
School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, England.
Coates
L
L
Newbold
R
R
Brindley
A A
AA
Stauffer
F
F
Beaven
G D E
GD
Gill
R
R
Coker
A
A
Wood
S P
SP
Warren
M J
MJ
Shoolingin-Jordan
P M
PM
Neier
R
R
Cooper
J B
JB
D000622:Aminolevulinic Acid / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D000623:Porphobilinogen Synthase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D012545:Schiff Bases
C505712:5-hydroxylaevulinic acid; D005656:Fungal Proteins; D012545:Schiff Bases; D000622:Aminolevulinic Acid; D000623:Porphobilinogen Synthase