This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Cofactors, Prosthetic Groups, Electron Carriers Biosynthesis → Tetrapyrrole Biosynthesis|
Some taxa known to possess this pathway include : Arabidopsis thaliana col , Escherichia coli K-12 substr. MG1655 , Euglena gracilis , Nicotiana tabacum , Pseudomonas denitrificans , Salmonella enterica enterica serovar Typhimurium , Triticum aestivum
Tetrapyrroles are compounds whose molecules have four rings of the pyrrole type, generally linked together by single-atom bridges between the alpha positions of the five-membered pyrrole rings. Tetrapyrroles function as a metal-binding cofactor in many important enzymes, proteins and pigments, such as heme, chlorophyll, cobalamine (vitamin B12), siroheme, and cofator F430. The biosynthesis of all of these cofactors start in a similar manner, with the production of the intermediate uroporphyrinogen-III. This intermediate is an important branch point: its methylation directs it toward siroheme, cobalamin or cofactor F430 synthesis, while decarboxylation directs it toward the synthesis of heme and chlorophyll [Phillips03].
The tetrapyrrole biosynthetic pathway shown here, which starts with glutamate, is found in plants, many bacteria (including Escherichia coli), and the archaea. A second tetrapyrrole biosynthetic pathway, which is found in animals, fungi, certain protozoans, and members of the α-proteobacteria, starts with glycine and succinyl-coA (see tetrapyrrole biosynthesis II (from glycine)). Interestingly, both pathways are present in the chloroplast-containing protozoan Euglena gracilis.
Regardless whether the starting point is glycine or glutamate, both pathways converge at the intermediate 5-aminolevulinate and proceed through the important intermediate uroporphyrinogen-III, which is a major branch point that leads to biosynthesis of different tetrapyrrole compounds, such as the corrinoid cobalamine (vitamin B12) (see MetaCyc pathway adenosylcobalamin biosynthesis II (late cobalt incorporation)), the methanogenic coenzyme F430 (see factor 430 biosynthesis), siroheme (see siroheme biosynthesis, and heme D.
Unification Links: EcoCyc:PWY-5188
Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554
Alwan89: Alwan AF, Mgbeje BI, Jordan PM (1989). "Purification and properties of uroporphyrinogen III synthase (co-synthase) from an overproducing recombinant strain of Escherichia coli K-12." Biochem J 264(2);397-402. PMID: 2557837
Avissar89: Avissar YJ, Beale SI (1989). "Identification of the enzymatic basis for delta-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli." J Bacteriol 171(6);2919-24. PMID: 2656630
Balg07: Balg C, Blais SP, Bernier S, Huot JL, Couture M, Lapointe J, Chenevert R (2007). "Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases." Bioorg Med Chem 15(1);295-304. PMID: 17049867
Banerjee04: Banerjee R, Dubois DY, Gauthier J, Lin SX, Roy S, Lapointe J (2004). "The zinc-binding site of a class I aminoacyl-tRNA synthetase is a SWIM domain that modulates amino acid binding via the tRNA acceptor arm." Eur J Biochem 271(4);724-33. PMID: 14764088
Bernier05: Bernier S, Dubois DY, Habegger-Polomat C, Gagnon LP, Lapointe J, Chenevert R (2005). "Glutamylsulfamoyladenosine and pyroglutamylsulfamoyladenosine are competitive inhibitors of E. coli glutamyl-tRNA synthetase." J Enzyme Inhib Med Chem 20(1);61-7. PMID: 15895686
Bollivar04: Bollivar DW, Clauson C, Lighthall R, Forbes S, Kokona B, Fairman R, Kundrat L, Jaffe EK (2004). "Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer." BMC Biochem 5;17. PMID: 15555082
Breton86: Breton R, Sanfacon H, Papayannopoulos I, Biemann K, Lapointe J (1986). "Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases." J Biol Chem 261(23);10610-7. PMID: 3015933
Brun90: Brun YV, Sanfacon H, Breton R, Lapointe J (1990). "Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW." J Mol Biol 214(4);845-64. PMID: 2201777
Cantoni84: Cantoni L, Dal Fiume D, Ruggieri R (1984). "Decarboxylation of uroporphyrinogen I and III in 2,3,7,8-tetrachlorodibenzo-p-dioxin induced porphyria in mice." Int J Biochem 16(5);561-5. PMID: 6724109
Curnow98: Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D (1998). "Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis." Proc Natl Acad Sci U S A 95(22);12838-43. PMID: 9789001
Dasgupta12: Dasgupta S, Manna D, Basu G (2012). "Structural and functional consequences of mutating a proteobacteria-specific surface residue in the catalytic domain of Escherichia coli GluRS." FEBS Lett 586(12);1724-30. PMID: 22584057
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Dubois04: Dubois DY, Blaise M, Becker HD, Campanacci V, Keith G, Giege R, Cambillau C, Lapointe J, Kern D (2004). "An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp." Proc Natl Acad Sci U S A 101(20);7530-5. PMID: 15096594
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