Tai CH - Search Results

1

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

Tai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF. Tai CH, et al. Biochemistry. 2001 Jun 26;40(25):7446-52. doi: 10.1021/bi015511s. Biochemistry. 2001. PMID: 11412097

2

Characterization of the S272A,D site-directed mutations of O-acetylserine sulfhydrylase: involvement of the pyridine ring in the alpha,beta-elimination reaction.

Daum S, Tai CH, Cook PF. Daum S, et al. Among authors: tai ch. Biochemistry. 2003 Jan 14;42(1):106-13. doi: 10.1021/bi0268044. Biochemistry. 2003. PMID: 12515544

3

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. Schnackerz KD, et al. Among authors: tai ch. Biochemistry. 1995 Sep 26;34(38):12152-60. doi: 10.1021/bi00038a008. Biochemistry. 1995. PMID: 7547955

4

Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies.

Tai CH, Nalabolu SR, Simmons JW 3rd, Jacobson TM, Cook PF. Tai CH, et al. Biochemistry. 1995 Sep 26;34(38):12311-22. doi: 10.1021/bi00038a027. Biochemistry. 1995. PMID: 7547974

5

Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants.

Tai CH, Nalabolu SR, Jacobson TM, Minter DE, Cook PF. Tai CH, et al. Biochemistry. 1993 Jun 29;32(25):6433-42. doi: 10.1021/bi00076a017. Biochemistry. 1993. PMID: 8518286

6

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

Woehl EU, Tai CH, Dunn MF, Cook PF. Woehl EU, et al. Among authors: tai ch. Biochemistry. 1996 Apr 16;35(15):4776-83. doi: 10.1021/bi952938o. Biochemistry. 1996. PMID: 8664267

7

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. Rege VD, et al. Among authors: tai ch. Biochemistry. 1996 Oct 15;35(41):13485-93. doi: 10.1021/bi961517j. Biochemistry. 1996. PMID: 8873618

8

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. Tai CH, et al. Biochemistry. 1998 Jul 28;37(30):10597-604. doi: 10.1021/bi980647k. Biochemistry. 1998. PMID: 9692949

9

O-acetylserine sulfhydrylase.

Tai CH, Cook PF. Tai CH, et al. Adv Enzymol Relat Areas Mol Biol. 2000;74:185-234. doi: 10.1002/9780470123201.ch5. Adv Enzymol Relat Areas Mol Biol. 2000. PMID: 10800596 Review.

10

Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound.

Burkhard P, Tai CH, Jansonius JN, Cook PF. Burkhard P, et al. Among authors: tai ch. J Mol Biol. 2000 Oct 20;303(2):279-86. doi: 10.1006/jmbi.2000.4109. J Mol Biol. 2000. PMID: 11023792

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