Purification and characterization of 5-aminolevulinic acid dehydratase from Methanosarcina barken
β Scribed by Suresh Bhosale; Deepa Kshirsagar; Prashant Pawar; Tulsiram Yeole; Dilip Ranade
- Book ID
- 109320517
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 454 KB
- Volume
- 127
- Category
- Article
- ISSN
- 0378-1097
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A full-length cDNA clone encoding tomato (Lycopersicon esculentum Mill.) 5-aminolevulinic acid dehydratase (ALAD) was isolated and characterized. The primary structure predicts a 430-amino acid precursor which comprises a 41.7 kDa, 388-amino acid mature protein and a 47-amino acid transit sequence.
The first intermediate substrate in the heme synthetic pathway, 5-aminolevulinic acid (ALA), is neurotoxic in animal models and may be responsible for some of the adverse neurologic outcomes in lead poisoning and porphyria in adult humans. ALA is a substrate for the enzyme aminolevulinic acid dehydr