关键词： 3′-phosphoadenosine-5′-phosphosulfate APR APS APS reductase ASU DLS PAPS Physcomitrella patens Sulfate assimilation Sulfonucleotide X-ray structure adenosine-5′-phosphosulfate adenosine-5′-phosphosulfate reductase asymmetric unit dynamic light scattering

Mesh ： Adenosine Phosphosulfate / chemistry Amino Acid Sequence Bryopsida / enzymology Catalytic Domain Conserved Sequence Crystallography, X-Ray Kinetics Models, Molecular Molecular Sequence Data Oxidoreductases Acting on Sulfur Group Donors / chemistry Plant Proteins / chemistry Protein Structure, Secondary Structural Homology, Protein Substrate Specificity

来  源：   DOI：10.1016/j.febslet.2013.09.034   PDF(Sci-hub)

Abstract：
Sulfonucleotide reductases catalyse the first reductive step of sulfate assimilation. Their substrate specificities generally correlate with the requirement for a [Fe4S4] cluster, where adenosine 5\'-phosphosulfate (APS) reductases possess a cluster and 3\'-phosphoadenosine 5\'-phosphosulfate reductases do not. The exception is the APR-B isoform of APS reductase from the moss Physcomitrella patens, which lacks a cluster. The crystal structure of APR-B, the first for a plant sulfonucleotide reductase, is consistent with a preference for APS. Structural conservation with bacterial APS reductase rules out a structural role for the cluster, but supports the contention that it enhances the activity of conventional APS reductases.
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