“Nicotianamine aminotransferase”的意思、由来-开放百科全书

词条

Nicotianamine aminotransferase

释义

References

{{enzyme
| Name = Nicotianamine aminotransferase
| EC_number = 2.6.1.80
| CAS_number =
| IUBMB_EC_number = 2/6/1/80
| GO_code =
| image =
| width =
| caption =
}}

In enzymology, a nicotianamine aminotransferase ({{EC number|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 -deamino-3-oxonicotianamine">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.

References

{{cite journal |author1 = Mori S | date = 1994 | title = Nicotianamine aminotransferase activities are correlated with the phytosiderophore secretions under Fe-deficient conditions in Gramineae | journal = J. Exp. Bot. | volume = 45 | pages = 1903–1906 | doi = 10.1093/jxb/45.12.1903 | last2 = Higuchi | first2 = Kyoko | last3 = Nishizawa | first3 = Naoko-Kishi | last4 = Fushiya | first4 = Shinji | last5 = Chino | first5 = Mitsuo | last6 = Mori | first6 = Satoshi | issue = 12 }}
{{cite journal | author = S | date = 1999 | title = Cloning Two Genes for Nicotianamine Aminotransferase, a Critical Enzyme in Iron Acquisition (Strategy II) in Graminaceous Plants | journal = Plant Physiol. | volume = 121 | pages = 947–56 | pmid = 10557244 | doi = 10.1104/pp.121.3.947 | last2 = Yamaguchi | first2 = H | last3 = Nakanishi | first3 = H | last4 = Shioiri | first4 = T | last5 = Nishizawa | first5 = NK | last6 = Mori | first6 = S | issue = 3 | pmc = 59459 }}
{{cite journal | vauthors = Schaaf G, Ludewig U, Erenoglu BE, Mori S, Kitahara T, von Wiren N | date = 2004 | title = ZmYS1 functions as a proton-coupled symporter for phytosiderophore- and nicotianamine-chelated metals | journal = J. Biol. Chem. | volume = 279 | pages = 9091–6 | pmid = 14699112 | doi = 10.1074/jbc.M311799200 | issue = 10 }}

2 : EC 2.6.1|Enzymes of unknown structure

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