Year |
Citation |
Score |
2012 |
Nemeria N, Binshtein E, Patel H, Balakrishnan A, Vered I, Shaanan B, Barak Z, Chipman D, Jordan F. Glyoxylate carboligase: a unique thiamin diphosphate-dependent enzyme that can cycle between the 4'-aminopyrimidinium and 1',4'-iminopyrimidine tautomeric forms in the absence of the conserved glutamate. Biochemistry. 51: 7940-52. PMID 22970650 DOI: 10.1021/Bi300893V |
0.456 |
|
2012 |
Belenky I, Steinmetz A, Vyazmensky M, Barak Z, Tittmann K, Chipman DM. Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I. The Febs Journal. 279: 1967-79. PMID 22443469 DOI: 10.1111/J.1742-4658.2012.08577.X |
0.495 |
|
2012 |
Barak Z, Chipman DM. Allosteric regulation in Acetohydroxyacid Synthases (AHASs)--different structures and kinetic behavior in isozymes in the same organisms. Archives of Biochemistry and Biophysics. 519: 167-74. PMID 22198286 DOI: 10.1016/J.Abb.2011.11.025 |
0.434 |
|
2011 |
Vyazmensky M, Steinmetz A, Meyer D, Golbik R, Barak Z, Tittmann K, Chipman DM. Significant catalytic roles for Glu47 and Gln 110 in all four of the C-C bond-making and -breaking steps of the reactions of acetohydroxyacid synthase II. Biochemistry. 50: 3250-60. PMID 21370850 DOI: 10.1021/Bi102051H |
0.479 |
|
2011 |
Slutzker A, Vyazmensky M, Chipman DM, Barak Z. Role of the C-terminal domain of the regulatory subunit of AHAS isozyme III: use of random mutagenesis with in vivo reconstitution (REM-ivrs). Biochimica Et Biophysica Acta. 1814: 449-55. PMID 21224018 DOI: 10.1016/J.Bbapap.2011.01.002 |
0.358 |
|
2010 |
Steinmetz A, Vyazmensky M, Meyer D, Barak ZE, Golbik R, Chipman DM, Tittmann K. Valine 375 and phenylalanine 109 confer affinity and specificity for pyruvate as donor substrate in acetohydroxy acid synthase isozyme II from Escherichia coli. Biochemistry. 49: 5188-99. PMID 20504042 DOI: 10.1021/Bi100555Q |
0.474 |
|
2009 |
Vyazmensky M, Zherdev Y, Slutzker A, Belenky I, Kryukov O, Barak Z, Chipman DM. Interactions between large and small subunits of different acetohydroxyacid synthase isozymes of Escherichia coli. Biochemistry. 48: 8731-7. PMID 19653643 DOI: 10.1021/Bi9009488 |
0.404 |
|
2009 |
Shaanan B, Chipman DM. Reaction mechanisms of thiamin diphosphate enzymes: new insights into the role of a conserved glutamate residue. The Febs Journal. 276: 2447-53. PMID 19476486 DOI: 10.1111/J.1742-4658.2009.06965.X |
0.404 |
|
2009 |
Chipman DM, Barak Z, Shaanan B, Vyazmensky M, Binshtein E, Belenky I, Temam V, Steinmetz A, Golbik R, Tittmann K. Origin of the specificities of acetohydroxyacid synthases and glyoxylate carboligase Journal of Molecular Catalysis B: Enzymatic. 61: 50-55. DOI: 10.1016/J.Molcatb.2009.03.015 |
0.437 |
|
2008 |
Shulman A, Zalyapin E, Vyazmensky M, Yifrach O, Barak Z, Chipman DM. Allosteric regulation of Bacillus subtilis threonine deaminase, a biosynthetic threonine deaminase with a single regulatory domain. Biochemistry. 47: 11783-92. PMID 18855421 DOI: 10.1021/Bi800901N |
0.39 |
|
2008 |
Kaplun A, Binshtein E, Vyazmensky M, Steinmetz A, Barak Z, Chipman DM, Tittmann K, Shaanan B. Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes. Nature Chemical Biology. 4: 113-8. PMID 18176558 DOI: 10.1038/Nchembio.62 |
0.439 |
|
2006 |
Kaplun A, Vyazmensky M, Zherdev Y, Belenky I, Slutzker A, Mendel S, Barak Z, Chipman DM, Shaanan B. Structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from Escherichia coli. Journal of Molecular Biology. 357: 951-63. PMID 16458324 DOI: 10.1016/J.Jmb.2005.12.077 |
0.358 |
|
2006 |
Vinogradov V, Vyazmensky M, Engel S, Belenky I, Kaplun A, Kryukov O, Barak Z, Chipman DM. Acetohydroxyacid synthase isozyme I from Escherichia coli has unique catalytic and regulatory properties. Biochimica Et Biophysica Acta. 1760: 356-63. PMID 16326011 DOI: 10.1016/J.Bbagen.2005.10.008 |
0.475 |
|
2005 |
Chipman DM, Duggleby RG, Tittmann K. Mechanisms of acetohydroxyacid synthases. Current Opinion in Chemical Biology. 9: 475-81. PMID 16055369 DOI: 10.1016/J.Cbpa.2005.07.002 |
0.47 |
|
2005 |
Vinogradov M, Kaplun A, Vyazmensky M, Engel S, Golbik R, Tittmann K, Uhlemann K, Meshalkina L, Barak Z, Hübner G, Chipman DM. Monitoring the acetohydroxy acid synthase reaction and related carboligations by circular dichroism spectroscopy. Analytical Biochemistry. 342: 126-33. PMID 15958189 DOI: 10.1016/J.Ab.2005.03.049 |
0.385 |
|
2005 |
Engel S, Vyazmensky M, Berkovich D, Barak Z, Merchuk J, Chipman DM. Column flow reactor using acetohydroxyacid synthase I from Escherichia coli as catalyst in continuous synthesis of R-phenylacetyl carbinol. Biotechnology and Bioengineering. 89: 733-40. PMID 15685598 DOI: 10.1002/Bit.20392 |
0.317 |
|
2005 |
Tittmann K, Vyazmensky M, Hübner G, Barak Z, Chipman DM. The carboligation reaction of acetohydroxyacid synthase II: steady-state intermediate distributions in wild type and mutants by NMR. Proceedings of the National Academy of Sciences of the United States of America. 102: 553-8. PMID 15640355 DOI: 10.1073/Pnas.0408210101 |
0.456 |
|
2004 |
Engel S, Vyazmensky M, Berkovich D, Barak Z, Chipman DM. Substrate range of acetohydroxy acid synthase I from Escherichia coli in the stereoselective synthesis of alpha-hydroxy ketones. Biotechnology and Bioengineering. 88: 825-31. PMID 15558598 DOI: 10.1002/Bit.20275 |
0.424 |
|
2004 |
Tittmann K, Schröder K, Golbik R, McCourt J, Kaplun A, Duggleby RG, Barak Z, Chipman DM, Hübner G. Electron transfer in acetohydroxy acid synthase as a side reaction of catalysis. Implications for the reactivity and partitioning of the carbanion/enamine form of (alpha-hydroxyethyl)thiamin diphosphate in a "nonredox" flavoenzyme. Biochemistry. 43: 8652-61. PMID 15236573 DOI: 10.1021/Bi049897T |
0.473 |
|
2004 |
Engel S, Vyazmensky M, Vinogradov M, Berkovich D, Bar-Ilan A, Qimron U, Rosiansky Y, Barak Z, Chipman DM. Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: catalysis of condensation with a specific ketoacid substrate. The Journal of Biological Chemistry. 279: 24803-12. PMID 15044456 DOI: 10.1074/Jbc.M401667200 |
0.453 |
|
2004 |
Porat I, Vinogradov M, Vyazmensky M, Lu CD, Chipman DM, Abdelal AT, Barak Z. Cloning and characterization of acetohydroxyacid synthase from Bacillus stearothermophilus. Journal of Bacteriology. 186: 570-4. PMID 14702326 DOI: 10.1128/Jb.186.2.570-574.2004 |
0.386 |
|
2003 |
Engel S, Vyazmensky M, Geresh S, Barak Z, Chipman DM. Acetohydroxyacid synthase: a new enzyme for chiral synthesis of R-phenylacetylcarbinol. Biotechnology and Bioengineering. 83: 833-40. PMID 12889023 DOI: 10.1002/Bit.10728 |
0.371 |
|
2003 |
Tittmann K, Golbik R, Uhlemann K, Khailova L, Schneider G, Patel M, Jordan F, Chipman DM, Duggleby RG, Hübner G. NMR analysis of covalent intermediates in thiamin diphosphate enzymes. Biochemistry. 42: 7885-91. PMID 12834340 DOI: 10.1021/Bi034465O |
0.458 |
|
2003 |
Zohar Y, Einav M, Chipman DM, Barak Z. Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones. Biochimica Et Biophysica Acta. 1649: 97-105. PMID 12818195 DOI: 10.1016/S1570-9639(03)00160-2 |
0.366 |
|
2003 |
Mendel S, Vinogradov M, Vyazmensky M, Chipman DM, Barak Z. The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli. Journal of Molecular Biology. 325: 275-84. PMID 12488095 DOI: 10.1016/S0022-2836(02)01142-7 |
0.415 |
|
2002 |
Kaplun A, Chipman DM, Barak Z. Isoleucine starvation caused by sulfometuron methyl in Salmonella typhimurium measured by translational frameshifting. Microbiology (Reading, England). 148: 713-7. PMID 11882705 DOI: 10.1099/00221287-148-3-713 |
0.345 |
|
2001 |
Bar-Ilan A, Balan V, Tittmann K, Golbik R, Vyazmensky M, Hübner G, Barak Z, Chipman DM. Binding and activation of thiamin diphosphate in acetohydroxyacid synthase. Biochemistry. 40: 11946-54. PMID 11570896 DOI: 10.1021/Bi0104524 |
0.462 |
|
2001 |
Mendel S, Elkayam T, Sella C, Vinogradov V, Vyazmensky M, Chipman DM, Barak Z. Acetohydroxyacid synthase: a proposed structure for regulatory subunits supported by evidence from mutagenesis. Journal of Molecular Biology. 307: 465-77. PMID 11243831 DOI: 10.1006/Jmbi.2000.4413 |
0.421 |
|
2000 |
Vyazmensky M, Elkayam T, Chipman DM, Barak Z. Isolation of subunits of acetohydroxy acid synthase isozyme III and reconstitution of holoenzyme. Methods in Enzymology. 324: 95-103. PMID 10989421 DOI: 10.1016/S0076-6879(00)24222-5 |
0.346 |
|
2000 |
Epelbaum S, Chipman DM, Barak Z. Analysis of intracellular metabolites as tool for studying branched-chain amino acid biosynthesis and its inhibition in bacteria Methods in Enzymology. 324: 10-23. PMID 10989413 DOI: 10.1016/S0076-6879(00)24214-6 |
0.321 |
|
2000 |
Engel S, Barak Z, Chipman DM, Merchuk JC. Purification of acetohydroxy acid synthase by separation in an aqueous two-phase system. Journal of Chromatography. B, Biomedical Sciences and Applications. 743: 281-6. PMID 10942298 DOI: 10.1016/S0378-4347(00)00053-0 |
0.356 |
|
2000 |
Engel S, Vyazmensky M, Barak Z, Chipman DM, Merchuk JC. Determination of the dissociation constant of valine from acetohydroxy acid synthase by equilibrium partition in an aqueous two-phase system. Journal of Chromatography. B, Biomedical Sciences and Applications. 743: 225-9. PMID 10942289 DOI: 10.1016/S0378-4347(00)00050-5 |
0.327 |
|
2000 |
Vyazmensky M, Barak Z, Chipman DM, Eichler J. Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 125: 205-10. PMID 10817907 DOI: 10.1016/S0305-0491(99)00170-4 |
0.444 |
|
1998 |
Epelbaum S, LaRossa RA, VanDyk TK, Elkayam T, Chipman DM, Barak Z. Branched-chain amino acid biosynthesis in Salmonella typhimurium: A quantitative analysis Journal of Bacteriology. 180: 4056-4067. PMID 9696751 DOI: 10.1128/Jb.180.16.4056-4067.1998 |
0.435 |
|
1998 |
Chipman D, Barak Z, Schloss JV. Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases. Biochimica Et Biophysica Acta. 1385: 401-19. PMID 9655946 DOI: 10.1016/S0167-4838(98)00083-1 |
0.465 |
|
1998 |
Peisach D, Chipman DM, Van Ophem PW, Manning JM, Ringe D. Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase. Biochemistry. 37: 4958-67. PMID 9538014 DOI: 10.1021/Bi972884D |
0.394 |
|
1998 |
Peisach D, Chipman DM, Van Ophem PW, Manning JM, Ringe D. D-Cycloserine inactivation of D-amino acid aminotransferase leads to a stable noncovalent protein complex with an aromatic cycloserine-PLP derivative Journal of the American Chemical Society. 120: 2268-2274. DOI: 10.2210/Pdb2Daa/Pdb |
0.341 |
|
1996 |
Ibdah M, Bar-Ilan A, Livnah O, Schloss JV, Barak Z, Chipman DM. Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis. Biochemistry. 35: 16282-91. PMID 8973202 DOI: 10.1021/Bi961588I |
0.424 |
|
1996 |
Vyazmensky M, Sella C, Barak Z, Chipman DM. Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Biochemistry. 35: 10339-46. PMID 8756689 DOI: 10.1021/Bi9605604 |
0.411 |
|
1996 |
Epelbaum S, Chipman DM, Barak Z. Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium Journal of Bacteriology. 178: 1187-1196. PMID 8576056 DOI: 10.1128/Jb.178.4.1187-1196.1996 |
0.411 |
|
1993 |
Sella C, Weinstock O, Barak Z, Chipman DM. Subunit association in acetohydroxy acid synthase isozyme III. Journal of Bacteriology. 175: 5339-43. PMID 8366022 DOI: 10.1128/Jb.175.17.5339-5343.1993 |
0.449 |
|
1993 |
Landstein D, Arad S, Barak Z, Chipman D. Relationships among the herbicide and functional sites of acetohydroxy acid synthase from Chlorella emersonii Planta. 191. DOI: 10.1007/Bf00240889 |
0.371 |
|
1992 |
Weinstock O, Sella C, Chipman DM, Barak Z. Properties of subcloned subunits of bacterial acetohydroxy acid synthases. Journal of Bacteriology. 174: 5560-6. PMID 1512191 DOI: 10.1128/Jb.174.17.5560-5566.1992 |
0.432 |
|
1990 |
Landstein D, Chipman DM, Arad SM, Barak Z. Acetohydroxy Acid Synthase Activity in Chlorella emersonii under Auto- and Heterotrophic Growth Conditions. Plant Physiology. 94: 614-20. PMID 16667756 DOI: 10.1104/Pp.94.2.614 |
0.398 |
|
1990 |
Gollop N, Damri B, Chipman DM, Barak Z. Physiological implications of the substrate specificities of acetohydroxy acid synthases from varied organisms. Journal of Bacteriology. 172: 3444-9. PMID 2345154 DOI: 10.1128/Jb.172.6.3444-3449.1990 |
0.374 |
|
1990 |
Epelbaum S, Chipman DM, Barak Z. Determination of products of acetohydroxy acid synthase by the colorimetric method, revisited Analytical Biochemistry. 191: 96-99. PMID 2077946 DOI: 10.1016/0003-2697(90)90393-N |
0.369 |
|
1989 |
Gollop N, Damri B, Barak Z, Chipman DM. Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli. Biochemistry. 28: 6310-7. PMID 2675968 DOI: 10.1021/Bi00441A024 |
0.469 |
|
1989 |
Markus S, Priel Z, Chipman DM. Interaction of calcium and vanadate with fluorescein isothiocyanate labeled Ca2+-ATPase from sarcoplasmic reticulum: Kinetics and equilibria Biochemistry. 28: 793-799. PMID 2523730 DOI: 10.1021/Bi00428A057 |
0.336 |
|
1988 |
Chipman DM, Jencks WP. Specificity of the sarcoplasmic reticulum calcium ATPase at the hydrolysis step. Biochemistry. 27: 5707-12. PMID 2972313 DOI: 10.1021/Bi00415A047 |
0.392 |
|
1987 |
Gollop N, Barak Z, Chipman DM. A method for simultaneous determination of the two possible products of acetohydroxy acid synthase. Analytical Biochemistry. 160: 323-31. PMID 3578759 DOI: 10.1016/0003-2697(87)90054-6 |
0.39 |
|
1987 |
Barak Z, Chipman DM, Gollop N. Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. Journal of Bacteriology. 169: 3750-6. PMID 3301814 DOI: 10.1128/Jb.169.8.3750-3756.1987 |
0.406 |
|
1986 |
Markus S, Priel Z, Chipman DM. Simultaneous binding of calcium and vanadate to the Ca2+ -ATPase of sarcoplasmic reticulum Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 874: 128-135. PMID 2945595 DOI: 10.1016/0167-4838(86)90109-3 |
0.373 |
|
1983 |
Gollop N, Chipman DM, Barak Z. Inhibition of acetohydroxy acid synthase by leucine. Biochimica Et Biophysica Acta. 748: 34-9. PMID 6351926 DOI: 10.1016/0167-4838(83)90024-9 |
0.324 |
|
1983 |
Chipman DM, Lev A. Modification of the conformational equilibria in the sodium and potassium dependent adenosinetriphosphatase with glutaraldehyde. Biochemistry. 22: 4450-9. PMID 6313040 DOI: 10.1021/Bi00288A016 |
0.402 |
|
1983 |
Chipman DM, Elhanany E, Berger R, Lev A. Alteration of Conformational Equilibria in Na,K-ATPase by Glutaraldehyde Treatment Current Topics in Membranes and Transport. 19: 471-476. DOI: 10.1016/S0070-2161(08)60597-3 |
0.331 |
|
1981 |
Odom TA, Chipman DM, Betts G, Bernhard SA. Transient and steady-state kinetic studies of sodium-potassium adenosine triphosphatase using β-(2-furyl)acryloyl phosphate as chromophoric substrate assay Biochemistry. 20: 480-486. PMID 6260131 DOI: 10.1021/Bi00506A006 |
0.457 |
|
1979 |
Shoshan V, Shavit N, Chipman DM. Kinetics of nucleotide binding to chloroplast coupling factor (CF1). Biochimica Et Biophysica Acta. 504: 108-22. PMID 152122 DOI: 10.1016/0005-2728(78)90010-5 |
0.36 |
|
1979 |
Banai M, Shavit N, Chipman DM. Specificity of nucleotide binding sites in isolated chloroplast coupling factor (CF1). Biochimica Et Biophysica Acta. 504: 100-7. PMID 152121 DOI: 10.1016/0005-2728(78)90009-9 |
0.32 |
|
1977 |
Schindler M, Assaf Y, Sharon N, Chipman DM. Mechanism of lysozyme catalysis: role of ground-state strain in subsite D in hen egg-white and human lysozymes. Biochemistry. 16: 423-31. PMID 13816 DOI: 10.1021/Bi00622A013 |
0.321 |
|
1974 |
Highsmith S, Chipman DM. Preparation of tritium-labeled hyaluronic acid oligomers and their use in enzyme studies Analytical Biochemistry. 61: 557-566. PMID 4417815 DOI: 10.1016/0003-2697(74)90424-2 |
0.368 |
|
1973 |
Van Eikeren P, White WA, Chipman DM. Synthesis of oligosaccharides containing 2-acetamido-2-deoxyxylose by chemical and enzymic methods The Journal of Organic Chemistry. 38: 1831-1836. DOI: 10.1021/Jo00950A013 |
0.391 |
|
1972 |
Steffens JJ, Cross JP, Chipman DM. Reactions of dihydronicotinamides II. The acid-catalyzed dimerization of 1-benzyl-1,4-dihydronicotinamide Tetrahedron Letters. 13: 4883-4886. DOI: 10.1016/S0040-4039(01)94456-9 |
0.344 |
|
1972 |
VAN EIKEREN P, CHIPMAN DM. ChemInform Abstract: SUBSTRAT-VERFORMUNG BEI DER KATALYSE DURCH LYSOZYM, RK. VON LYSOZYM MIT OLIGOSACCHARIDEN, DIE N-ACETYL-XYLOSAMIN ENTHALTEN Chemischer Informationsdienst. 3. DOI: 10.1002/Chin.197238392 |
0.302 |
|
1965 |
Breslow R, Chipman D. Mixed metal complexes as enzyme models. I. Intracomplex nucleophilic catalysis by an oxime anion. Journal of the American Chemical Society. 87: 4195-4196. PMID 5845280 DOI: 10.1021/Ja01096A039 |
0.503 |
|
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