Biology:Adenylylsulfate—ammonia adenylyltransferase
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Short description: Class of enzymes
| Adenylylsulfate-ammonia adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.7.51 | ||||||||
| CAS number | 79121-94-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Adenylylsulfate-ammonia adenylyltransferase (EC 2.7.7.51) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme characterised from Chlorella converts 5'-adenylyl sulfate to adenosine 5'-phosphoramidat by reaction with ammonia. Sulfate is a byproduct.[1][2][3] This enzyme activity has been reported to be a general property of fragile histidine triad proteins.[4]
This enzyme is a transferase, specifically one transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is adenylyl-sulfate:ammonia adenylyltransferase. Other names in common use include APSAT, and adenylylsulfate:ammonia adenylyltransferase.[5]
References
- ↑ "Adenylyl sulfate (APS):ammonia adenylyl transferase (APSAT) forming adenosine 5' phosphoramidate (APA) from APS and ammonia". Plant Physiol. 63S: 162. 1979.
- ↑ "Further purification and properties of adenylyl sulfate (APS): ammonia adenylyl transferase (APSAT) from Chlorella". Plant Physiol. 65S: 17. 1980.
- ↑ Chauncey, Thomas R.; Uhteg, Lawrence C.; Westley, John (1987). "Thiosulfate reductase". Sulfur and Sulfur Amino Acids. Methods in Enzymology. 143. pp. 350–354. doi:10.1016/0076-6879(87)43062-0. ISBN 978-0-12-182043-5.
- ↑ Wojdyła-Mamoń, Anna M.; Guranowski, Andrzej (2015). "Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins". Bioscience Reports 35 (4). doi:10.1042/BSR20150135. PMID 26181368.
- ↑ Enzyme 2.7.7.51 at KEGG Pathway Database.
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