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Table representation of search results timeline featuring number of search results per year.
Year | Number of Results |
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2002 | 1 |
2006 | 1 |
2010 | 1 |
2011 | 2 |
2016 | 1 |
2024 | 0 |
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Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity.
FEBS Lett. 2016 Sep;590(17):2991-6. doi: 10.1002/1873-3468.12325. Epub 2016 Aug 9.
FEBS Lett. 2016.
PMID: 27447465
Free article.
Roles of the redox-active disulfide and histidine residues forming a catalytic dyad in reactions catalyzed by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Kofoed MA, Wampler DA, Pandey AS, Peters JW, Ensign SA.
Kofoed MA, et al.
J Bacteriol. 2011 Sep;193(18):4904-13. doi: 10.1128/JB.05231-11. Epub 2011 Jul 15.
J Bacteriol. 2011.
PMID: 21764916
Free PMC article.
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Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Pandey AS, Mulder DW, Ensign SA, Peters JW.
Pandey AS, et al.
FEBS Lett. 2011 Feb 4;585(3):459-64. doi: 10.1016/j.febslet.2010.12.035. Epub 2010 Dec 27.
FEBS Lett. 2011.
PMID: 21192936
Free article.
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Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW.
Pandey AS, et al.
Biochemistry. 2006 Jan 10;45(1):113-20. doi: 10.1021/bi051518o.
Biochemistry. 2006.
PMID: 16388586
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Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW.
Nocek B, et al.
Biochemistry. 2002 Oct 29;41(43):12907-13. doi: 10.1021/bi026580p.
Biochemistry. 2002.
PMID: 12390015
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