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Results 1 - 10 of 26 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33763704 Protein complex formation in methionine chain-elongation and leucine biosynthesis Sci. Rep. 11 3524 2021 Arabidopsis thaliana 33568694
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33763704 Protein complex formation in methionine chain-elongation and leucine biosynthesis Sci. Rep. 11 3524 2021 Arabidopsis thaliana Col0 33568694
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33677727 A leuC mutation leading to increased L-lysine production and rel-independent global expression changes in Corynebacterium glutamicum Appl. Microbiol. Biotechnol. 72 783-789 2006 Corynebacterium glutamicum 16944136
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33677727 A leuC mutation leading to increased L-lysine production and rel-independent global expression changes in Corynebacterium glutamicum Appl. Microbiol. Biotechnol. 72 783-789 2006 Corynebacterium glutamicum B-6 16944136
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33706255 Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation Plant Mol. Biol. 71 227-239 2009 Arabidopsis thaliana 19597944
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33706255 Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation Plant Mol. Biol. 71 227-239 2009 Arabidopsis thaliana Col-0 19597944
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33701510 Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the small subunit of isopropylmalate isomerase (Rv2987c) from Mycobacterium tuberculosis Acta Crystallogr. Sect. F 65 136-139 2009 Mycobacterium tuberculosis 19194004
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33701510 Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the small subunit of isopropylmalate isomerase (Rv2987c) from Mycobacterium tuberculosis Acta Crystallogr. Sect. F 65 136-139 2009 Mycobacterium tuberculosis H37Rv 19194004
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33729127 Crystal structure of LeuD from Methanococcus jannaschii Biochem. Biophys. Res. Commun. 419 160-164 2012 Methanocaldococcus jannaschii 22326391
Show all pathways known for 4.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.33722946 Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme J. Mol. Biol. 344 325-333 2004 Pyrococcus horikoshii 15522288
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