Biology:Nicotianamine aminotransferase
From HandWiki
| Nicotianamine aminotransferase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.6.1.80 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a nicotianamine aminotransferase (EC 2.6.1.80) is an enzyme that catalyzes the chemical reaction
- nicotianamine + 2-oxoglutarate [math]\displaystyle{ \rightleftharpoons }[/math] 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.
References
- Mori S; Higuchi, Kyoko; Nishizawa, Naoko-Kishi; Fushiya, Shinji; Chino, Mitsuo; Mori, Satoshi (1994). "Nicotianamine aminotransferase activities are correlated with the phytosiderophore secretions under Fe-deficient conditions in Gramineae". J. Exp. Bot. 45 (12): 1903–1906. doi:10.1093/jxb/45.12.1903.
- S; Yamaguchi, H; Nakanishi, H; Shioiri, T; Nishizawa, NK; Mori, S (1999). "Cloning Two Genes for Nicotianamine Aminotransferase, a Critical Enzyme in Iron Acquisition (Strategy II) in Graminaceous Plants". Plant Physiol. 121 (3): 947–56. doi:10.1104/pp.121.3.947. PMID 10557244.
- "ZmYS1 functions as a proton-coupled symporter for phytosiderophore- and nicotianamine-chelated metals". J. Biol. Chem. 279 (10): 9091–6. 2004. doi:10.1074/jbc.M311799200. PMID 14699112.
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