Similar articles for PMID: 11412090

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1

Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions.

Liu M, Sergienko EA, Guo F, Wang J, Tittmann K, Hübner G, Furey W, Jordan F. Liu M, et al. Biochemistry. 2001 Jun 26;40(25):7355-68. doi: 10.1021/bi002855u. Biochemistry. 2001. PMID: 11412090

2

Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products.

Sergienko EA, Jordan F. Sergienko EA, et al. Biochemistry. 2001 Jun 26;40(25):7369-81. doi: 10.1021/bi002856m. Biochemistry. 2001. PMID: 11412091

3

Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values.

Sergienko EA, Jordan F. Sergienko EA, et al. Biochemistry. 2001 Jun 26;40(25):7382-403. doi: 10.1021/bi002857e. Biochemistry. 2001. PMID: 11412092

4

Effects of substitution of tryptophan 412 in the substrate activation pathway of yeast pyruvate decarboxylase.

Li H, Jordan F. Li H, et al. Biochemistry. 1999 Aug 3;38(31):10004-12. doi: 10.1021/bi9902440. Biochemistry. 1999. PMID: 10433707

5

Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase.

Wang J, Golbik R, Seliger B, Spinka M, Tittmann K, Hübner G, Jordan F. Wang J, et al. Biochemistry. 2001 Feb 13;40(6):1755-63. doi: 10.1021/bi001003r. Biochemistry. 2001. PMID: 11327837

6

Role of glutamate 91 in information transfer during substrate activation of yeast pyruvate decarboxylase.

Li H, Furey W, Jordan F. Li H, et al. Biochemistry. 1999 Aug 3;38(31):9992-10003. doi: 10.1021/bi9902438. Biochemistry. 1999. PMID: 10433706

7

Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylase.

Balakrishnan A, Gao Y, Moorjani P, Nemeria NS, Tittmann K, Jordan F. Balakrishnan A, et al. J Am Chem Soc. 2012 Feb 29;134(8):3873-85. doi: 10.1021/ja211139c. Epub 2012 Feb 17. J Am Chem Soc. 2012. PMID: 22300533 Free PMC article.

8

Is a hydrophobic amino acid required to maintain the reactive V conformation of thiamin at the active center of thiamin diphosphate-requiring enzymes? Experimental and computational studies of isoleucine 415 of yeast pyruvate decarboxylase.

Guo F, Zhang D, Kahyaoglu A, Farid RS, Jordan F. Guo F, et al. Biochemistry. 1998 Sep 22;37(38):13379-91. doi: 10.1021/bi9807097. Biochemistry. 1998. PMID: 9748345

9

The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography.

Canyuk B, Focia PJ, Eakin AE. Canyuk B, et al. Biochemistry. 2001 Mar 6;40(9):2754-65. doi: 10.1021/bi001195q. Biochemistry. 2001. PMID: 11258886

10

Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants, with substitution of adjacent active center acidic groups from different subunits, display restored activity.

Sergienko EA, Jordan F. Sergienko EA, et al. Biochemistry. 2002 May 14;41(19):6164-9. doi: 10.1021/bi0121712. Biochemistry. 2002. PMID: 11994012

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