Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference59 articles.
1. Comparative stability and catalytic and chemical properties of the sulfate-activating enzymes from Penicillium chrysogenum (mesophile) and Penicillium duponti (thermophile)
2. ATP sulfurylase from Penicillium chrysogenum. Molecular basis of the sigmoidal velocity curves induced by sulfhydryl group modification.
3. The “regulatory” sulfhydryl group of Penicillium chrysogenum ATP sulfurylase
4. Regulation of inorganic sulfate activation in filamentous fungi. Allosteric inhibition of ATP sulfurylase by 3'-phosphoadenosine-5'-phosphosulfate.
5. Rat liver ATP-sulfurylase: Purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions
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