Detail of "9026-94-2"
- CAS Number:
- 9026-94-2
- Name:
Aldolase,phospho-2-keto-3-deoxyheptonate
- Synonyms:
- 2-Dehydro-3-deoxyphosphoheptonatealdolase; 2-Keto-3-arabinoheptulosonate 7-phosphate synthase;2-Keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase;2-keto-3-Deoxy-D-arabino heptonate-7-phosphate synthetase;3-Deoxy-7-phosphoheptulonate synthase; 3-Deoxy-D-arabino-2-heptulosonic acid7-phosphate synthetase; 3-Deoxy-D-arabino-heptolosonate-7-phosphate synthase;3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase;3-Deoxy-D-arabino-heptulosonate 7-phosphate synthetase;3-Deoxy-D-arabino-heptulosonic acid 7-phosphate synthase;3-Deoxy-D-arabino-heptulosonic acid 7-phosphate synthase;3-Deoxy-D-arabinoheptulosonate-7-phosphate synthase; AminoDAHP synthase; DAHPsynthase; DAHP synthetase; Deoxy-D-arabinoheptulosonate-7-phosphate synthase;E.C. 2.5.1.54; E.C. 4.1.2.15; Phospho-2-keto-3-deoxyheptonate aldolase;Phospho-2-keto-3-deoxyheptonic aldolase; Phospho-2-oxo-3-deoxyheptonatealdolase
Aldolase,phospho-2-keto-3-deoxyheptonate
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Reference
- The nucleotide sequence of the aroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
- The nucleotide sequence of the aroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Shultz, John; Hermodson, Mark A.; Garner, Craig C.; Herrmann, Klaus M. (Dep. Biochem., Purdue Univ., West Lafayette, IN 47907, USA). J. Biol. Chem., 259(15), 9655-61 (English) 1984. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Genetics) Section cross-reference(s): 7 The translated sequence of aroF, the 1st structural gene of the tyrosine operon of E. coli, was detd. The 1068 nucleotides encode the 356 amino acids that form the subunit of the dimeric tyrosine-sensitive 3-deoxyarabinoheptulosonate 7-phosphate synthase (I) [9026-94-2]. The primary structure of I was confirmed by automated Edman degrdn. of peptide fragments produced by cleavage with CnBr, limited trypsin digestion, Staphylococcus aureus strain V8 protease, or mild acid hydrolysis. The amino acids sequence of I is compared with the sequence of the phenylalanine-sensitive I, deduced from the aroG DNA sequence.
- Cloning of the ARO3 gene of Saccharomyces cerevisiae and its regulation
- Cloning of the ARO3 gene of Saccharomyces cerevisiae and its regulation. Teshiba, Sadao; Furter, Rolf; Niederberger, Peter; Braus, Gerhard; Paravicini, Gerhard; Huetter, Ralf (Mikrobiol. Inst., Eidg. Tech. Hochsch., Zurich CH-8092, Switz.). MGG, Mol. Gen. Genet., 205(2), 353-7 (English) 1986. CODEN: MGGEAE. ISSN: 0026-8925. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Genetics) Section cross-reference(s): 7, 10 Regulation of the 2 isozymes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (DAHP synthase; EC 4.1.2.15) [9026-94-2] encoded by the genes ARO3 and ARO4 of S. cerevisiae was studied. Both genes respond equally well to the general control of amino acid biosynthesis. Strains with mutations in these 2 genes were obtained by selecting first for a single aro3 mutation and afterwards for a double aro3 aro4 mutation. Gene ARO3, coding for the phenylanine-dependent isozyme of DAHP synthase, was cloned on the 2-mm multicopy vector pJDB207 by complementation of mutation aro3-1 in yeast. The ARO3 gene, carried originally on a 9.6-kb BamHI fragment (plasmid pME541A), was subcloned on a 1.9-kb HindIII-XbaI fragment (plasmid pME543). A transcript of ~1.5 kb was shown to proceed from the HindIII towards the XbaI site. Expression from the 9.6-kb as well as from the 1.9-kb fragment was normal on a multicopy vector, since in both cases DAHP synthase levels of ~50-fold the wild-type level were obsd.

