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| PROSITE documentation PDOC00153 |
Delta-aminolevulinic acid dehydratase active site
Description:
Delta-aminolevulinic acid dehydratase (EC 4.2.1.24) (ALAD) [1] catalyzes the
second step in the biosynthesis of heme, the condensation of two molecules of
5-aminolevulinate to form porphobilinogen. The enzyme is an oligomer composed
of eight identical subunits. Each of the subunits binds an atom of zinc or of
magnesium (in plants). A lysine has been implicated in the catalytic mechanism
[2]. The sequence of the region in the vicinity of the active site residue
is conserved in ALAD from various prokaryotic and eukaryotic species.
Last update:
November 1995 / Pattern and text revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| D_ALA_DEHYDRATASE, PS00169; Delta-aminolevulinic acid dehydratase active site (PATTERN) |
| Consensus pattern: |
G-x-D-x-[LIVM](2)-[IV]-K-P-[GSA]-x(2)-Y
K is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE |
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| Matching PDB structures:
1AW5 1B4E 1B4K 1E51 ... [ALL] |
References:
| 1 |
Authors | Li J.-M., Russell C.S., Cosloy S.D. |
| Title | The structure of the Escherichia coli hemB gene. |
| Source | Gene 75:177-184(1989). |
| PubMed ID | 2656410 |
| 2 |
Authors | Gibbs P.N.B., Jordan P.M. |
| Title | Identification of lysine at the active site of human 5-aminolaevulinate dehydratase. |
| Source | Biochem. J. 236:447-451(1986). |
| PubMed ID | 3092810 |
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