InChI=1S/C6H12N4O3/c7-3(5(12)13)4(11)2-1-9-6(8)10-2/h2-4,11H,1,7H2,(H,12,13)(H3,8,9,10)/t2-,3-,4-/m0/s1 |
RFBWLSHSKDHIQO-HZLVTQRSSA-N |
[H][C@]1(CNC(=N)N1)[C@H](O)[C@H](N)C(O)=O |
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Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
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View more via ChEBI Ontology
(3R)-3-[(4S)-2-iminoimidazolidin-4-yl]-L-serine
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Haltli B, Tan Y, Magarvey NA, Wagenaar M, Yin X, Greenstein M, Hucul JA, Zabriskie TM (2005) Investigating beta-hydroxyenduracididine formation in the biosynthesis of the mannopeptimycins. Chemistry & biology 12, 1163-1168 [PubMed:16298295] [show Abstract] The mannopeptimycins (MPPs) are potent glycopeptide antibiotics that contain both D and L forms of the unique, arginine-derived amino acid beta-hydroxyenduracididine (betahEnd). The product of the mppO gene in the MPP biosynthetic cluster resembles several non-heme iron, alpha-ketoglutarate-dependent oxygenases, such as VioC and clavaminate synthase. The role of MppO in betahEnd biosynthesis was confirmed through inactivation of mppO, which yielded a strain that produced dideoxy-MPPs, indicating that mppO is essential for generating the beta-hydroxy functionality for both betahEnd residues. Characterization in vitro of recombinant His6-MppO expressed in E. coli revealed that MppO selectively hydroxylates the beta carbon of free L-enduracididine. |
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