3kox

Structural highlights

Function

OAME_ACESD Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. OraE may be the catalytic subunit. Active only on D-ornithine and 2,4-diaminopentanoic acid but not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D-alpha-lysine.^{[1] [2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Aminomutase 3D structures

References

1. ↑ Chen HP, Wu SH, Lin YL, Chen CM, Tsay SS. Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-ornithine aminomutase from Clostridium sticklandii. J Biol Chem. 2001 Nov 30;276(48):44744-50. Epub 2001 Sep 27. PMID:11577113 doi:http://dx.doi.org/10.1074/jbc.M108365200
2. ↑ Somack R, Costilow RN. Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D- -ornithine 5,4-aminomutase. Biochemistry. 1973 Jul 3;12(14):2597-604. PMID:4711468
3. ↑ Somack R, Costilow RN. Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D- -ornithine 5,4-aminomutase. Biochemistry. 1973 Jul 3;12(14):2597-604. PMID:4711468