D-Tagatose 6-Phosphate Pathways1
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چکیده
Lactose is usually metabolized by A-galactosidase-catalyzed cleavage to D-glucose and D-galactose, followed by the conversion of Dgalactose to D-glucose 6-phosphate via the well known Leloir pathway (10): D-galactose *D galactose 1-phosphate D-glucose 1-phosphate D-glucose 6-phosphate. In Staphylococcus aureus, however, the disaccharide is utilized exclusively via lactose phosphate, which is cleaved by a phospho-a-galactosidase to yield D-glucose and D-galactose 6-phosphate (5-7). The metabolism of exogenous D-galactose is also initiated by phosphorylation at C6 (13). DGalactose 6-phosphate is metabolized further through tagatose derivatives by a pathway recently elucidated in our laboratory (1): D-galactose 6-phosphate -* D-tagatose 6-phosphate D-tagatose 1, 6-diphosphate D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate. Other organisms besides S. aureus reported to possess phospho-,B-galactosidase activity are the group N streptococci, and these bacteria have also been shown to possess f-galactosidase (9). We have now examined representatives of this group to determine whether the occurrence of the tagatose 6-phosphate pathway extends to these organisms. In contrast to other organisms, we show here that the group N streptococci possess the enzymes of both pathways of Dgalactose metabolism. Escherichia coli B/r and Aerobacter aerogenes PRL-R3 were grown aerobically at 37 and 32 C, respectively, in a mineral medium (4) supplemented with 0.5% of the indicated sugar. Cell extracts were prepared by sonic disruption of cellular suspensions (4). S. aureus NCTC 8511 was grown and extracts were prepared as described previously (1). Streptococcus lactis ATCC 7962, S. lactis ATCC 11454, and S.
منابع مشابه
Lactose and D-galactose metabolism in Staphylococcus aureus. II. Isomerization of D-galactose 6-phosphate to D-tagatose 6-phosphate by a specific D-galactose-6-phosphate isomerase.
The inducible D-galactose-6-phosphate isomerase that functions in the metabolism of lactose and D-galactose in Staphylococcus aureus was partially purified from extracts of D-galactose-grown cells. It was shown to catalyze specifically the reversible isomerization of D-galactose 6-phosphate to D-tagatose 6-phosphate, the apparent Km values being 9.6 mM and 1.9 mM, respectively. At equilibrium, ...
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DNA cloned into Escherichia coli K-12 from a serotype c strain of Streptococcus mutans encodes three enzyme activities for galactose utilization via the tagatose 6-phosphate pathway: galactose 6-phosphate isomerase, tagatose 6-phosphate kinase, and tagatose-1,6-bisphosphate aldolase. The genes coding for the tagatose 6-phosphate pathway were located on a 3.28-kb HindIII DNA fragment. Analysis o...
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The tagatose 6-phosphate pathway gene cluster (lacABCD) encoding galactose-6-phosphate isomerase, tagatose-6-phosphate kinase, and tagatose-1,6-diphosphate aldolase of Lactococcus lactis subsp. lactis MG1820 has been characterized by cloning, nucleotide sequence analysis, and enzyme assays. Transcription studies showed that the four tagatose 6-phosphate pathway genes are the first genes of the ...
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D-Galactose-6-phosphate isomerase from Lactobacillus rhamnosus (LacAB; EC 5.3.1.26), which is encoded by the tagatose-6-phosphate pathway gene cluster (lacABCD), catalyzes the isomerization of D-galactose-6-phosphate to D-tagatose-6-phosphate during lactose catabolism and is used to produce rare sugars as low-calorie natural sweeteners. The crystal structures of LacAB and its complex with D-tag...
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The sugar phosphate specificity of the active site of 6-phosphofructo-2-kinase and of the inhibitory site of fructose-2,6-bisphosphatase was investigated. The Michaelis constants and relative Vmax values of the sugar phosphates for the 6-phosphofructo-2-kinase were: D-fructose 6-phosphate, Km = 0.035 mM, Vmax = 1; L-sorbose 6-phosphate, Km = 0.175 mM, Vmax = 1.1; D-tagatose 6-phosphate, Km = 15...
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