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Results 1 - 10 of 88 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157762386 Mutational analysis to identify the residues essential for the acetyltransferase activity of GlmU in Bacillus subtilis RSC Adv. 7 13858-13867 2017 Escherichia coli -
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157762386 Mutational analysis to identify the residues essential for the acetyltransferase activity of GlmU in Bacillus subtilis RSC Adv. 7 13858-13867 2017 Bacillus subtilis -
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157762386 Mutational analysis to identify the residues essential for the acetyltransferase activity of GlmU in Bacillus subtilis RSC Adv. 7 13858-13867 2017 Bacillus subtilis 168 -
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288685 Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis J. Bacteriol. 176 5788-5795 1994 Bacillus subtilis 8083170
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288685 Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis J. Bacteriol. 176 5788-5795 1994 Escherichia coli 8083170
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288685 Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis J. Bacteriol. 176 5788-5795 1994 Escherichia coli JM83 8083170
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Bacillus subtilis 9733680
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Escherichia coli 9733680
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Neisseria gonorrhoeae 9733680
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Escherichia coli JM83 9733680
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