|
|
|
|
| LEADER |
01330 am a22002653u 4500 |
| 001 |
24094 |
| 042 |
|
|
|a dc
|
| 100 |
1 |
0 |
|a Erskine, P.T.
|e author
|
| 700 |
1 |
0 |
|a Coates, L.
|e author
|
| 700 |
1 |
0 |
|a Newbold, R.
|e author
|
| 700 |
1 |
0 |
|a Brindley, A.A.
|e author
|
| 700 |
1 |
0 |
|a Stauffer, F.
|e author
|
| 700 |
1 |
0 |
|a Beaven, G.D.E
|e author
|
| 700 |
1 |
0 |
|a Gill, R.
|e author
|
| 700 |
1 |
0 |
|a Coker, A.
|e author
|
| 700 |
1 |
0 |
|a Wood, S.P.
|e author
|
| 700 |
1 |
0 |
|a Warren, M.J.
|e author
|
| 700 |
1 |
0 |
|a Shoolingin-Jordan, P.M.
|e author
|
| 700 |
1 |
0 |
|a Neier, R.
|e author
|
| 700 |
1 |
0 |
|a Cooper, J.B.
|e author
|
| 245 |
0 |
0 |
|a Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid
|
| 260 |
|
|
|c 2005.
|
| 856 |
|
|
|z Get fulltext
|u https://eprints.soton.ac.uk/24094/1/Coker2_05.pdf
|
| 520 |
|
|
|a 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 Å . 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).
|
| 655 |
7 |
|
|a Article
|
