Nicotianamine aminotransferase
From Wikipedia, the free encyclopedia
In enzymology, a nicotianamine aminotransferase (EC 2.6.1.80) is an enzyme that catalyzes the chemical reaction
- nicotianamine + 2-oxoglutarate 3"-deamino-3"-oxonicotianamine + L-glutamate
Thus, the two substrates of this enzyme are nicotianamine and 2-oxoglutarate, whereas its two products are [[3-deamino-3-oxonicotianamine]] and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is nicotianamine:2-oxoglutarate aminotransferase; nicotianamine transaminase. Other names in common use include NAAT, NAAT-I, NAAT-II, and NAAT-III.
[edit] References
- IUBMB entry for 2.6.1.80
- BRENDA references for 2.6.1.80 (Recommended.)
- PubMed references for 2.6.1.80
- PubMed Central references for 2.6.1.80
- Google Scholar references for 2.6.1.80
- and Mori S (1994). "Nicotianamine aminotransferase activities are correlated with the phytosiderophore secretions under Fe-deficient conditions in Gramineae". J. Exp. Bot. 45: 1903–1906. doi: .
- S (1999). "Cloning two genes for nicotianamine aminotransferase, a critical enzyme in iron acquisition (Strategy II) in graminaceous plants". Plant. Physiol. 121: 947–56. doi: . PMID 10557244.
- Schaaf G, Ludewig U, Erenoglu BE, Mori S, Kitahara T, von Wiren N (2004). "ZmYS1 functions as a proton-coupled symporter for phytosiderophore- and nicotianamine-chelated metals". J. Biol. Chem. 279: 9091–6. doi: . PMID 14699112.