Literature DB >> 16904

Specificity of 2-keto-3-deoxygluconate-6-P aldolase for open chain form of 2-keto-3-deoxygluconate-6-P.

C F Midelfort, R K Gupta, H P Meloche.   

Abstract

2-Keto-3-deoxygluconate-6-P exists as an euqilibrium of three forms at 25 degrees measurable by 13C NMR: alpha-furanose anomer (41%), beta-furanose anomer (50%), and open chain keto (9%). The three forms are interconverted rapidly (greater than 0.5 s-1) so that the unidirectional rates of furanose ring opening and closing can be quantitated by an NMR line broadening method. The 2-keto-3-deoxygluconate aldolase is specific for only one of these forms, the open chain keto form. The rates for ring opening calculated from the rapid kinetic enzyme system compare closely with those obtained with the NMR method.

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Year:  1977        PMID: 16904

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  2 in total

1.  Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates.

Authors:  Manoj Cheriyan; Eric J Toone; Carol A Fierke
Journal:  Protein Sci       Date:  2007-11       Impact factor: 6.725

2.  Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases.

Authors:  Suzanne Wolterink-van Loo; André van Eerde; Marco A J Siemerink; Jasper Akerboom; Bauke W Dijkstra; John van der Oost
Journal:  Biochem J       Date:  2007-05-01       Impact factor: 3.857

  2 in total

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