|
|
| |
2.3.1.37 |
| Activity |
2.3.1.37 |
| Description |
5-aminolevulinic acid synthase. |
| Notes |
A very compact and distinct family of enzymes from eukarya (fungi-metazoa) and eubacteria. |
| PDB |
1H7J;1H7D; |
| PLP Fold Type |
I |
| PLP-dependent Domain |
|
| Number of sequences |
30 |
| Sequences in seed alignment |
|
| Reference sequence |
HEM0_MOUSE |
| Domain interval |
189-536 |
| Catalytic site |
391 K |
| | |
| References |
Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW. (2005) Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans EMBO J 24 3166-77. Elrod, S.L.; Jones, A.; Berka, R.M.; Cherry, J.R. (2000) Cloning of the Aspergillus oryzae 5-aminolevulinate synthase gene and its use as a selectable marker Curr Genet 38 291-98. Bolt, E. L.; Kryszak, L.; Zeilstra-Ryalls, J.; Shoolingin-Jordan, P. M.; Warren, M. J. (1999) Characterization of the rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes, HemA and HemT, isolated from recombinant Escherichia coli Eur J Biochem 265 290-9. Ferreira, G. C.; Dailey, H. A. (1993) Expression of mammalian 5-aminolevulinate synthase in Escherichia coli. Overproduction, purification, and characterization J Biol Chem 268 584-90. Articles on 2.3.1.37 |
| last changed |
2008/05/20 11:50 |
|