1j5p

Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolutionCrystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution

Structural highlights

1j5p is a 1 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	TM1643 (ATCC 43589)
Activity:	L-aspartate oxidase, with EC number 1.4.3.16
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[ASPD_THEMA] Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Does not show aspartate oxidase activity. Is also able to catalyze the reverse reaction, i.e. the reductive amination of oxaloacetate.^[1]

Evolutionary Conservation

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

References

↑ Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, Tong L. Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J Biol Chem. 2003 Mar 7;278(10):8804-8. Epub 2002 Dec 21. PMID:12496312 doi:10.1074/jbc.M211892200

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, Tong L. Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J Biol Chem. 2003 Mar 7;278(10):8804-8. Epub 2002 Dec 21. PMID:12496312 doi:10.1074/jbc.M211892200

[1]