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Results 1 - 10 of 14 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the reaction diagram Show all sequences 4.99.1.9739547 Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin Proc. Natl. Acad. Sci. USA 112 2210-2215 2015 Bacillus subtilis 25646457
Display the reaction diagram Show all sequences 4.99.1.9739547 Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin Proc. Natl. Acad. Sci. USA 112 2210-2215 2015 Cutibacterium acnes 25646457
Display the reaction diagram Show all sequences 4.99.1.9739547 Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin Proc. Natl. Acad. Sci. USA 112 2210-2215 2015 Mycobacterium tuberculosis 25646457
Display the reaction diagram Show all sequences 4.99.1.9738499 Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes J. Bacteriol. 174 8081-8093 1992 Bacillus subtilis 1459957
Display the reaction diagram Show all sequences 4.99.1.9738499 Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes J. Bacteriol. 174 8081-8093 1992 Bacillus subtilis 168 1459957
Display the reaction diagram Show all sequences 4.99.1.9738498 The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation J. Bacteriol. 174 3953-3963 1992 Salmonella enterica subsp. enterica serovar Typhimurium 1317844
Display the reaction diagram Show all sequences 4.99.1.934963 Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis Eur. J. Biochem. 220 201-208 1994 Bacillus subtilis 8119288
Display the reaction diagram Show all sequences 4.99.1.9771056 Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase FEBS J. 287 2779-2796 2020 Listeria monocytogenes 31794133
Display the reaction diagram Show all sequences 4.99.1.9771075 Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups FEBS J. 289 1680-1699 2022 Listeria monocytogenes 34719106
Display the reaction diagram Show all sequences 4.99.1.9775669 Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III propionate interactions and porphyrin core deformation Protein Sci. 32 e4534 2023 Listeria monocytogenes 36479958
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