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Items: 1 to 20 of 142

1.

Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.

Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R.

J Mol Biol. 1999 Jun 18;289(4):991-1002.

PMID:
10369777
2.

Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase.

Hadfield A, Shammas C, Kryger G, Ringe D, Petsko GA, Ouyang J, Viola RE.

Biochemistry. 2001 Dec 4;40(48):14475-83.

PMID:
11724560
3.

The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae.

Viola RE, Liu X, Ohren JF, Faehnle CR.

Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):321-30. doi: 10.1107/S0907444907068552. Epub 2008 Feb 20.

PMID:
18323627
4.

Expansion of the aspartate beta-semialdehyde dehydrogenase family: the first structure of a fungal ortholog.

Arachea BT, Liu X, Pavlovsky AG, Viola RE.

Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):205-12. doi: 10.1107/S0907444909052834. Epub 2010 Jan 22.

PMID:
20124701
5.

Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum.

Scapin G, Reddy SG, Blanchard JS.

Biochemistry. 1996 Oct 22;35(42):13540-51.

PMID:
8885833
6.

A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae.

Blanco J, Moore RA, Kabaleeswaran V, Viola RE.

Protein Sci. 2003 Jan;12(1):27-33.

7.
8.

Structures of ternary complexes of aspartate-semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis H37Rv.

Vyas R, Tewari R, Weiss MS, Karthikeyan S.

Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):671-9. doi: 10.1107/S0907444912007330. Epub 2012 May 17.

PMID:
22683789
9.

High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase.

Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK.

J Mol Biol. 2004 Aug 13;341(3):797-806.

PMID:
15288787
10.

Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway.

Sivaraman J, Li Y, Banks J, Cane DE, Matte A, Cygler M.

J Biol Chem. 2003 Oct 31;278(44):43682-90. Epub 2003 Aug 1.

11.
12.

A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii.

Faehnle CR, Ohren JF, Viola RE.

J Mol Biol. 2005 Nov 11;353(5):1055-68. Epub 2005 Sep 29.

PMID:
16225889
13.

The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.

Blanco J, Moore RA, Faehnle CR, Coe DM, Viola RE.

Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1388-95. Epub 2004 Jul 21.

PMID:
15272161
14.

Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase.

Blanco J, Moore RA, Viola RE.

Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12613-7. Epub 2003 Oct 14.

15.
16.

The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.

Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF.

J Biol Chem. 2003 May 23;278(21):19176-82. Epub 2003 Mar 6.

17.

Critical catalytic functional groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.

Blanco J, Moore RA, Faehnle CR, Viola RE.

Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1808-15. Epub 2004 Sep 23.

PMID:
15388927
18.

Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643.

Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, Tong L.

J Biol Chem. 2003 Mar 7;278(10):8804-8. Epub 2002 Dec 21.

19.

Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase.

Fujii T, Maeda M, Mihara H, Kurihara T, Esaki N, Hata Y.

Biochemistry. 2000 Feb 15;39(6):1263-73.

PMID:
10684605
20.

Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms.

Kai Y, Matsumura H, Izui K.

Arch Biochem Biophys. 2003 Jun 15;414(2):170-9. Review.

PMID:
12781768

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