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Volumn 353, Issue 1, 2011, Pages 89-99

Redesign of the phosphate binding site of L -rhamnulose- 1-phosphate aldolase towards a dihydroxyacetone dependent aldolase

Author keywords

aldol reaction; amino aldehydes; enzyme catalysis; L rhamnulose 1 phosphate aldolase; mutagenesis

Indexed keywords


EID: 79251498939     PISSN: 16154150     EISSN: 16154169     Source Type: Journal    
DOI: 10.1002/adsc.201000719     Document Type: Article
Times cited : (40)

References (73)
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    • This result was observed with either RhuA[Zn(II)] or RhuA[Co(II)].
    • This result was observed with either RhuA[Zn(II)] or RhuA[Co(II)].
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    • L -Ribulose-5-phosphate 4-epimerase (AraD, EC 5.1.3.4) from E. coli, a class II enzyme closely related to FucA, and variants of this enzyme displayed a background activity on the aldol addition reaction of DHA to glycolaldehyde; see.
    • L -Ribulose-5-phosphate 4-epimerase (AraD, EC 5.1.3.4) from E. coli, a class II enzyme closely related to FucA, and variants of this enzyme displayed a background activity on the aldol addition reaction of DHA to glycolaldehyde; see, J. Samuel, Y. Luo, P. M. Morgan, N. C. J. Strynadka, M. E. Tanner, Biochemistry 2001, 40, 14772-14780.
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    • Aldol addition of DHA to 2 catalyzed by L -fuculose-1-phosphate aldolase failed, indicating that DHA acceptance appears to be an exclusive property of RhuA.
    • Aldol addition of DHA to 2 catalyzed by L -fuculose-1-phosphate aldolase failed, indicating that DHA acceptance appears to be an exclusive property of RhuA.
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    • An accurate treatment of the kinetic data would require the use of the Michaelis-Menten model for two-substrate reactions. Under these conditions the determined ${V{{app\hfill \atop {\rm max}\hfill}}}$ and ${K{{app\hfill \atop {\rm m}\hfill}}}$, depended on the concentration of the acceptor aldehyde, which is fixed, (see, Wiley-VCH Verlag GmbH, Weinheim, pp ) thus allowing comparison of the kinetic properties among the different enzymes, as stated in the text.
    • An accurate treatment of the kinetic data would require the use of the Michaelis-Menten model for two-substrate reactions. Under these conditions the determined ${V{{app\hfill \atop {\rm max}\hfill}}}$ and ${K{{app\hfill \atop {\rm m}\hfill}}}$, depended on the concentration of the acceptor aldehyde, which is fixed, (see, H. Bisswanger, Enzyme Kinetics: Principles and Methods, Wiley-VCH Verlag GmbH, Weinheim, 2002, pp 108-119) thus allowing comparison of the kinetic properties among the different enzymes, as stated in the text.
    • (2002) Enzyme Kinetics: Principles and Methods , pp. 108-119
    • Bisswanger, H.1
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    • note
    • [32]). When other acceptors are used, different reaction rates were obtained, suggesting that the rate-limiting step would be the aldol addition.
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    • Tampa, Florida Free pdf of the paper
    • K. J. Bowers, E. Chow, H. Xu, R. O. Dror, M. P. Eastwood, B. A. Gregersen, J. L. Klepeis, I. Kolossváry, M. A. Moraes, F. D. Sacerdoti, J. K. Salmon, Y. Shan, D. E. Shaw, Proceedings of the ACM/IEEE Conference on Supercomputing (SC06), Tampa, Florida, 2006. Free pdf of the paper:.
    • (2006) Proceedings of the ACM/IEEE Conference on Supercomputing (SC06)
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.