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Items: 1 to 20 of 727

1.

Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate.

Tai CH, Yoon MY, Kim SK, Rege VD, Nalabolu SR, Kredich NM, Schnackerz KD, Cook PF.

Biochemistry. 1998 Jul 28;37(30):10597-604.

PMID:
9692949
2.

Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes.

Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, Campanini B, Bettati S, Mozzarelli A, Rabeh WM, Li L, Cook PF.

Biochemistry. 2007 Jul 17;46(28):8315-30.

PMID:
17583914
3.

Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction.

Tai CH, Rabeh WM, Guan R, Schnackerz KD, Cook PF.

Arch Biochem Biophys. 2008 Apr 15;472(2):115-25. doi: 10.1016/j.abb.2008.01.021.

PMID:
18275838
5.

A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst.

Rege VD, Kredich NM, Tai CH, Karsten WE, Schnackerz KD, Cook PF.

Biochemistry. 1996 Oct 15;35(41):13485-93.

PMID:
8873618
6.

Formation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase.

Woehl EU, Tai CH, Dunn MF, Cook PF.

Biochemistry. 1996 Apr 16;35(15):4776-83.

PMID:
8664267
8.

Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway.

Strambini GB, Cioni P, Cook PF.

Biochemistry. 1996 Jun 25;35(25):8392-400.

PMID:
8679597
9.

Structure and mechanism of O-acetylserine sulfhydrylase.

Rabeh WM, Cook PF.

J Biol Chem. 2004 Jun 25;279(26):26803-6. Review.

10.

Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A.

Tian H, Guan R, Salsi E, Campanini B, Bettati S, Kumar VP, Karsten WE, Mozzarelli A, Cook PF.

Biochemistry. 2010 Jul 27;49(29):6093-103. doi: 10.1021/bi100473v.

PMID:
20550197
12.
14.

Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction.

Schnackerz KD, Tai CH, Simmons JW 3rd, Jacobson TM, Rao GS, Cook PF.

Biochemistry. 1995 Sep 26;34(38):12152-60.

PMID:
7547955
15.

Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylase.

Hwang CC, Woehl EU, Minter DE, Dunn MF, Cook PF.

Biochemistry. 1996 May 21;35(20):6358-65.

PMID:
8639581
16.

Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction.

Rabeh WM, Alguindigue SS, Cook PF.

Biochemistry. 2005 Apr 12;44(14):5541-50.

PMID:
15807548
17.

Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase.

Tai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF.

Biochemistry. 2001 Jun 26;40(25):7446-52.

PMID:
11412097
18.

Mutation of cysteine 111 in Dopa decarboxylase leads to active site perturbation.

Dominici P, Moore PS, Castellani S, Bertoldi M, Voltattorni CB.

Protein Sci. 1997 Sep;6(9):2007-15.

19.

(31)P NMR studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium.

Guan R, Nimmo SA, Schnackerz KD, Cook PF.

Arch Biochem Biophys. 2009 Jul 15;487(2):85-90. doi: 10.1016/j.abb.2009.05.016.

PMID:
19501038
20.
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