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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 2.3.1.157288687 Purification, crystallization and preliminary x-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase Acta Crystallogr. Sect. D 57 296-297 2001 Escherichia coli 11173485
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157701468 Structure and function of GlmU from Mycobacterium tuberculosis Acta Crystallogr. Sect. D 65 275-283 2009 Mycobacterium tuberculosis 19237750
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157701468 Structure and function of GlmU from Mycobacterium tuberculosis Acta Crystallogr. Sect. D 65 275-283 2009 Mycobacterium tuberculosis H37Rv 19237750
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157735396 GlmU (N-acetylglucosamine-1-phosphate uridyltransferase) bound to three magnesium ions and ATP at the active site Acta Crystallogr. Sect. F 70 703-708 2014 Mycobacterium tuberculosis 24915076
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157735396 GlmU (N-acetylglucosamine-1-phosphate uridyltransferase) bound to three magnesium ions and ATP at the active site Acta Crystallogr. Sect. F 70 703-708 2014 Mycobacterium tuberculosis ATCC 25618 24915076
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157701520 Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group Acta Crystallogr. Sect. F 65 435-439 2009 Mycobacterium tuberculosis 19407371
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157701520 Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group Acta Crystallogr. Sect. F 65 435-439 2009 Mycobacterium tuberculosis H37Rv 19407371
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157746844 Improvement of ST0452 N-acetylglucosamine-1-phosphate uridyltransferase activity by the cooperative effect of two single mutations identified through structure-based protein engineering Appl. Environ. Microbiol. 84 e002213-18 2018 Sulfurisphaera tokodaii 30291121
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157746844 Improvement of ST0452 N-acetylglucosamine-1-phosphate uridyltransferase activity by the cooperative effect of two single mutations identified through structure-based protein engineering Appl. Environ. Microbiol. 84 e002213-18 2018 Sulfurisphaera tokodaii DSM 16993 30291121
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157755852 Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase activities of the archaeal ST0452 protein through site saturation mutagenesis of the 97th amino acid position Appl. Environ. Microbiol. 83 e02291-16 2017 Sulfurisphaera tokodaii 27864169
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