| http://purl.uniprot.org/citations/7410392 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7410392 | http://www.w3.org/2000/01/rdf-schema#comment | "The inducible D-ketohexose-1,6-diphosphate aldolase that functions in the metabolism of lactose and D-galactose in Staphylococcus aurues was purified to electrophoretic homogeneity from an extract of D-galactose-grown cells. At saturating substrate concentrations, D-tagatose 1,6-diphosphate was cleaved to dihydroxyacetone phosphate plus D-glyceraldehyde 3-phosphate at twice the rate of D-fructose 1,6-diphosphate; Km values for D-tagatose 1,6-diphosphate and D-fructose 12,6-diphosphate were 1.5 mM and 2.5 mM, respectively. The enzyme catalyzed the aldol condensation of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate to yield a mixture of the 1,6-diphosphate derivatives of D-tagatose, D-fructose, D-sorbose, and D-psicose, indicating that it also catalyzes the cleavage of all four D-2-ketohexose 1,6-diphosphates. The enzyme was not inhibited by EDTA and it had no divalent metal ion requirement, but it did exhibit substrate-dependent inactivation by NaBH4, indicating that it is a Class I (Schiff's base) aldolase. Density gradient centrifugation and gel electrophoresis in the presence of sodium dodecyl sulfate indicated that the enzyme exists as a monomer with amolecular weight of about 37,000 and a sedimentation coefficient of 3.4 S. Data on the stability, pH optimum, and inducibility of the enzyme are also presented."xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)43564-8"xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://purl.uniprot.org/core/author | "Anderson R.L."xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://purl.uniprot.org/core/author | "Bissett D.L."xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://purl.uniprot.org/core/date | "1980"xsd:gYear |
| http://purl.uniprot.org/citations/7410392 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://purl.uniprot.org/core/pages | "8750-8755"xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://purl.uniprot.org/core/title | "Lactose and D-galactose metabolism in Staphylococcus aureus. IV. Isolation and properties of a class I D-ketohexose-1,6-diphosphate aldolase that catalyzes the cleavage of D-tagatose 1,6-diphosphate."xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://purl.uniprot.org/core/volume | "255"xsd:string |
| http://purl.uniprot.org/citations/7410392 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7410392 |
| http://purl.uniprot.org/citations/7410392 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7410392 |
| http://purl.uniprot.org/uniprot/#_P0A010-mappedCitation-7410392 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/7410392 |
| http://purl.uniprot.org/uniprot/P0A010 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/7410392 |