BRENDA - Enzyme Database show

Study of 5-aminolevulinate dehydratase in radish seedlings: are there housekeeping and light-induced enzymes?

Berthe, T.; Klein-Eude, D.; Balange, A.P.; Plant Sci. 164, 395-405 (2003)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
Raphanus sativus
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.24
Raphanus sativus
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
653558
Raphanus sativus
porphobilinogen + 2 H2O
-
653558
Raphanus sativus
?
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
Raphanus sativus
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
653558
Raphanus sativus
porphobilinogen + 2 H2O
-
653558
Raphanus sativus
?