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pro vyhledávání: '"Ajay Singh Tanwar"'
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e77781 (2013)
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) is a 140 kDa bi-functional enzyme involved in a coupled reaction, where the glutaminase active site produces ammonia that is subsequently utilized to convert FGAR to its corresponding amidin
Externí odkaz:
https://doaj.org/article/69cee2ef50614263914e6d8c160a69a9
Publikováno v:
Biochemistry. 52:3512-3522
NE0047 from Nitrosomonas europaea has been annotated as a zinc-dependent deaminase; however, the substrate specificity is unknown because of the low level of structural similarity and sequence identity compared to other family members. In this study,
Publikováno v:
IndraStra Global.
Molecular tunnels in enzyme systems possess variable architecture and are therefore difficult to predict. In this work, we design and apply an algorithm to resolve the pathway followed by ammonia using the bifunctional enzyme formylglycinamide ribonu
Communication between the two catalytic domains of formylglycinamide ribonucleotide amidotransferase
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 73:C1176-C1176
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 68(Pt 6)
Formylglycinamide ribonucleotide (FGAR) amidotransferase (FGAR-AT) takes part in purine biosynthesis and is a multidomain enzyme with multiple spatially separated active sites. FGAR-AT contains a glutaminase domain that is responsible for the generat
Publikováno v:
'PloS One ', vol: 8, pages: e77781-1-e77781-13 (2013)
PLoS ONE, Vol 8, Iss 11, p e77781 (2013)
PLoS ONE
PLoS ONE, Vol 8, Iss 11, p e77781 (2013)
PLoS ONE
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) is a 140 kDa bi-functional enzyme involved in a coupled reaction, where the glutaminase active site produces ammonia that is subsequently utilized to convert FGAR to its corresponding amidin