Literature summary extracted from

Berthe, T.; Klein-Eude, D.; Balange, A.P.
Study of 5-aminolevulinate dehydratase in radish seedlings: are there housekeeping and light-induced enzymes? (2003), Plant Sci., 164, 395-405.

No PubMed abstract available

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
4.2.1.24	5-aminolevulinate + 5-aminolevulinate	Raphanus sativus	the enzyme catalyzes the third step of tetrapyrrole synthesis leading to the formation of heme and chlorophylls in plant tissues. In the light, both 5-aminolevulinate dehydratase activity, and protein level increases 3-4 times compared to the dark-control level. However, no change in the amount of related mRNA is observed. The apparent stability of the mRNA can be due to the abundant expression of a housekeeping gene, which shadows a related gene expressed in the light	porphobilinogen + 2 H2O	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.2.1.24	Raphanus sativus	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.2.1.24	5-aminolevulinate + 5-aminolevulinate	the enzyme catalyzes the third step of tetrapyrrole synthesis leading to the formation of heme and chlorophylls in plant tissues. In the light, both 5-aminolevulinate dehydratase activity, and protein level increases 3-4 times compared to the dark-control level. However, no change in the amount of related mRNA is observed. The apparent stability of the mRNA can be due to the abundant expression of a housekeeping gene, which shadows a related gene expressed in the light	Raphanus sativus	porphobilinogen + 2 H2O	-	?

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Release 2023.1 (January 2023)