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Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima.
Yang X, Ma K. Yang X, et al. J Bacteriol. 2007 Apr;189(8):3312-7. doi: 10.1128/JB.01525-06. Epub 2007 Feb 9. J Bacteriol. 2007. PMID: 17293421 Free PMC article.
The V(max) was 230 +/- 14 mumol/min/mg (k(cat)/K(m) = 548,000 min(-1) mM(-1)), and the K(m) values for NADH and oxygen were 42 +/- 3 and 43 +/- 4 muM, respectively. ...
The V(max) was 230 +/- 14 mumol/min/mg (k(cat)/K(m) = 548,000 min(-1) mM(-1)), and the K(m) values for NADH and oxygen …
NAD(P)H:rubredoxin oxidoreductase from Pyrococcus furiosus.
Ma K, Adams MW. Ma K, et al. Methods Enzymol. 2001;334:55-62. doi: 10.1016/s0076-6879(01)34458-0. Methods Enzymol. 2001. PMID: 11398485 No abstract available.
Ferredoxin:NADP oxidoreductase from Pyrococcus furiosus.
Ma K, Adams MW. Ma K, et al. Methods Enzymol. 2001;334:40-5. doi: 10.1016/s0076-6879(01)34456-7. Methods Enzymol. 2001. PMID: 11398480 No abstract available.
Alcohol dehydrogenases from Thermococcus litoralis and Thermococcus strain ES-1.
Ma K, Adams MW. Ma K, et al. Methods Enzymol. 2001;331:195-201. doi: 10.1016/s0076-6879(01)31057-1. Methods Enzymol. 2001. PMID: 11265461 No abstract available.
Hydrogenases I and II from Pyrococcus furiosus.
Ma K, Adams MW. Ma K, et al. Methods Enzymol. 2001;331:208-16. doi: 10.1016/s0076-6879(01)31059-5. Methods Enzymol. 2001. PMID: 11265463 No abstract available.
Characterization of acetohydroxyacid synthase from the hyperthermophilic bacterium Thermotoga maritima.
Eram MS, Sarafuddin B, Gong F, Ma K. Eram MS, et al. Biochem Biophys Rep. 2015 Aug 28;4:89-97. doi: 10.1016/j.bbrep.2015.08.014. eCollection 2015 Dec. Biochem Biophys Rep. 2015. PMID: 29124191 Free PMC article.
The apparent K(m) and V(max) for pyruvate were 16.4±2 mM and 246±7 U/mg, respectively. Reconstitution of the catalytic and regulatory subunits led to increased AHAS activity. ...
The apparent K(m) and V(max) for pyruvate were 16.4±2 mM and 246±7 U/mg, respectively. Reconstitution of the catalytic and regulatory …
In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus.
Grunden AM, Jenney FE Jr, Ma K, Ji M, Weinberg MV, Adams MW. Grunden AM, et al. Appl Environ Microbiol. 2005 Mar;71(3):1522-30. doi: 10.1128/AEM.71.3.1522-1530.2005. Appl Environ Microbiol. 2005. PMID: 15746356 Free PMC article.
Towards the crystal structure of glycerol dehydrogenase from Thermotoga maritima.
Srinivasan V, Ma K, Adams MW, Newton MG, Rose JP, Wang BC. Srinivasan V, et al. Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):867-9. doi: 10.1107/s0907444902005012. Epub 2002 Apr 26. Acta Crystallogr D Biol Crystallogr. 2002. PMID: 11976506
Characterization of a zinc-containing alcohol dehydrogenase with stereoselectivity from the hyperthermophilic archaeon Thermococcus guaymasensis.
Ying X, Ma K. Ying X, et al. J Bacteriol. 2011 Jun;193(12):3009-19. doi: 10.1128/JB.01433-10. Epub 2011 Apr 22. J Bacteriol. 2011. PMID: 21515780 Free PMC article.
The kinetic parameters of the enzyme showed that the apparent K(m) values and catalytic efficiency for NADPH were 40 times lower and 5 times higher than those for NADP(+), respectively. ...
The kinetic parameters of the enzyme showed that the apparent K(m) values and catalytic efficiency for NADPH were 40 times lower and …
Characterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima.
Yang X, Ma K. Yang X, et al. J Bacteriol. 2010 Mar;192(5):1370-6. doi: 10.1128/JB.01035-09. Epub 2010 Jan 8. J Bacteriol. 2010. PMID: 20061476 Free PMC article.
The apparent K(m) values were determined to be 89 +/- 1.1 microM, 73 +/- 1.6 microM, and 780 +/- 20 microM for benzyl viologen, NADH, and NADPH, respectively. ...
The apparent K(m) values were determined to be 89 +/- 1.1 microM, 73 +/- 1.6 microM, and 780 +/- 20 microM for benzyl viologen, NADH, …
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