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• W2019908669 abstract "A synthetic gene specifying a putative 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans directed the synthesis of a 22.5 kDa peptide in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity by two chromatographic steps and was shown to catalyze the formation of L-3,4-dihydroxy-2-butanone 4-phosphate from ribulose 5-phosphate at a rate of 332 nmol mg(-1) min(-1). Hydrodynamic studies indicated a native molecular mass of 41 kDa in line with a homodimer structure. The protein was crystallized in its apoform. Soaking yielded crystals in complex with the substrate ribulose 5-phosphate. The structures were solved at resolutions of 1.6 and 1.7 angstroms, respectively, using 3,4-dihydroxy-2-butanone 4-phosphate synthase of E. coli for molecular replacement. Structural comparison with the orthologs of Magnaporthe grisea and Methanococcus jannaschii revealed a hitherto unknown conformation of the essential acidic active-site loop." @default.
• W2019908669 created "2016-06-24" @default.
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• W2019908669 date "2004-08-01" @default.
• W2019908669 modified "2023-10-16" @default.
• W2019908669 title "Potential Anti-infective Targets in Pathogenic Yeasts: Structure and Properties of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans" @default.
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• W2019908669 doi "https://doi.org/10.1016/j.jmb.2004.06.053" @default.
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