Akhtar M (1991) Mechanism and stereochemistry of the enzymes involved in the conversion of uroporphyrinogen III into haem. In: Jordan PM (ed) Biosynthesis of tetrapyrroles. Elsevier, Amsterdam, pp 67–99
Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer L (1998) The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J Mol Biol 284:401–419
Article
CAS
PubMed
Google Scholar
Al-Karadaghi S, Hansson M, Nikonov S, Jonsson B, Hederstedt L (1997) Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure 5:1501–1510
CAS
PubMed
Google Scholar
Arnould S, Camadro J-M (1998) The domain structure of protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides. Proc Natl Acad Sci USA 95:10553–10558
Article
CAS
PubMed
Google Scholar
Avissar YJ, Ormerod JG, Beale SI (1989) Distribution of delta-aminolevulinic acid biosynthetic pathways among phototrophic bacterial groups. Arch Microbiol 151:513–519
CAS
PubMed
Google Scholar
Beale SI (1999) Enzymes of chlorophyll biosynthesis. Photosynth Res 60:43–73
Article
CAS
Google Scholar
Beale SI, Castelfranco PA (1973) 14C incorporation from exogenous compounds into δ-aminolevulinic acid by greening cucumber cotyledons. Biochem Biophys Res Commun 52:143–149
CAS
PubMed
Google Scholar
Benjamin WH Jr, Hall P, Briles DE (1991) A hemA mutation renders Salmonella typhimurium avirulent in mice, yet capable of eliciting protection against intravenous infection with S. typhimurium. Microb Pathog 11:289–295
PubMed
Google Scholar
Bykhovskii V, Zaitseva NI, Eliseev AA (1998) Tetrapyrroles: diversity, biosynthesis, biotechnology. Appl Biochem Microbiol 34:1–18
Google Scholar
Chang CK (1994) Haem d1 and other haem cofactors from bacteria. Ciba Found Symp 180:228––246
CAS
PubMed
Google Scholar
Colloc'h N, Mornon JP, Camadro JM (2002) Towards a new T-fold protein?: the coproporphyrinogen III oxidase sequence matches many structural features from urate oxidase. FEBS Lett 526:5–10
Article
CAS
PubMed
Google Scholar
Contestabile R, Angelaccio S, Maytum R, Bossa F, John RA (2000a) The contribution of a conformationally mobile, active site loop to the reaction catalyzed by glutamate semialdehyde aminomutase. J Biol Chem 275:3879–3886
Article
CAS
PubMed
Google Scholar
Contestabile R, Jenn T, Akhtar M, Gani D, John RA (2000b) Reactions of glutamate 1-semialdehyde aminomutase with R- and S-enantiomers of a novel, mechanism-based inhibitor, 2,3-diaminopropyl sulfate. Biochemistry 39:3091–3096
Article
CAS
PubMed
Google Scholar
Dailey HA (2002) Terminal steps of haem biosynthesis. Biochem Soc Trans 30:590–595
CAS
PubMed
Google Scholar
Elder GH (1998) Update on enzyme and molecular defects in porphyria. Photodermatol Photoimmunol Photomed 14:66–69
CAS
PubMed
Google Scholar
Erskine PT, Senior N, Awan S, Lambert R, Lewis G, Tickle IJ, Sarwar M, Spencer P, Thomas P, Warren MJ, Shoolingin-Jordan PM, Wood SP, Cooper JB (1997) X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase. Nat Struct Biol 4:1025–1031
CAS
PubMed
Google Scholar
Erskine PT, Norton E, Cooper JB, Lambert R, Coker A, Lewis G, Spencer P, Sarwar M, Wood SP, Warren MJ, Shoolingin-Jordan PM (1999) X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 Å resolution. Biochemistry 38:4266–4276
Article
CAS
PubMed
Google Scholar
Frankenberg N, Lagarias JC (2003) Biosynthesis and biological functions of bilins. In: Kadish KM, Smith KM, Guilard R (eds) The porphyrin handbook. Elsevier, Amsterdam
Frankenberg N, Erskine PT, Cooper JB, Shoolingin-Jordan PM, Jahn D, Heinz DW (1999a) High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase. J Mol Biol 289:591–602
Article
CAS
PubMed
Google Scholar
Frankenberg N, Jahn D, Jaffe EK (1999b) Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions. Biochemistry 38:13976–13982
Article
CAS
PubMed
Google Scholar
Frere F, Schubert WD, Stauffer F, Frankenberg N, Neier R, Jahn D, Heinz DW (2002) Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism. J Mol Biol 320:237–247
PubMed
Google Scholar
Friedmann HC, Duban ME, Valasinas A, Frydman B (1992) The enantioselective participation of (S)- and (R)-diaminovaleric acids in the formation of delta-aminolevulinic acid in cyanobacteria. Biochem Biophys Res Commun 185:60–68
CAS
PubMed
Google Scholar
Fuchs J, Weber S, Kaufmann R (2000) Genotoxic potential of porphyrin type photosensitizers with particular emphasis on 5-aminolevulinic acid: implications for clinical photodynamic therapy. Free Radic Biol Med 28:537–548
Article
CAS
PubMed
Google Scholar
Gibson KD, Laver WG, Neuberger A (1958) Initial steps in the biosynthesis of porphyrins. The formation of δ-aminolevulinic acid from glycine and succinyl-CoA by particles of chicken erythrocytes. Biochem J 70:71–81
CAS
Google Scholar
Grimm B, Smith MA, von Wettstein D (1992) The role of Lys272 in the pyridoxal 5-phosphate active site of Synechococcus glutamate-1-semialdehyde aminotransferase. Eur J Biochem 206:579–585
CAS
PubMed
Google Scholar
Hadener A, Matzinger PK, Malashkevich VN, Louie GV, Wood SP, Oliver P, Alefounder PR, Pitt AR, Abell C, Battersby AR (1993) Purification, characterization, crystallisation and X-ray analysis of selenomethionine-labelled hydroxymethylbilane synthase from Escherichia coli. Eur J Biochem 211:615–624
CAS
PubMed
Google Scholar
Hadener A, Matzinger PK, Battersby AR, McSweeney S, Thompson AW, Hammersley AP, Harrop SJ, Cassetta A, Deacon A, Hunter WN, Nieh YP, Raftery J, Hunter N, Helliwell JR (1999) Determination of the structure of seleno-methionine-labelled hydroxymethylbilane synthase in its active form by multi-wavelength anomalous dispersion. Acta Crystallogr D Biol Crystallogr 55:631–643
Article
PubMed
Google Scholar
Hansson M, Hederstedt L (1994) Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX. J Bacteriol 176:5962–5970
CAS
PubMed
Google Scholar
Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN (1997) Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity. Proc Natl Acad Sci USA 94:4866–4871
Article
CAS
PubMed
Google Scholar
Heurgue-Hamard V, Champ S, Engstrom A, Ehrenberg M, Buckingham RH (2002) The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors. EMBO J 21:769–778
Article
CAS
PubMed
Google Scholar
Homuth G, Rompf A, Schumann W, Jahn D (1999) Transcriptional control of Bacillus subtilis hemN and hemZ. J Bacteriol 181:5922–5929
CAS
PubMed
Google Scholar
Hörtensteiner S (1999) Chlorophyll breakdown in higher plants and algae. Cell Mol Life Sci 56:330–347
Article
PubMed
Google Scholar
Hunter GA, Ferreira GC (1999a) Lysine-313 of 5-aminolevulinate synthase acts as a general base during formation of the quinonoid reaction intermediates. Biochemistry 38:3711–3718
Article
CAS
PubMed
Google Scholar
Hunter GA, Ferreira GC (1999b) Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release. J Biol Chem 274:12222–12228
Article
CAS
PubMed
Google Scholar
Ilag LL, Jahn D (1992) Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R. Biochemistry 31:7143–7151
CAS
PubMed
Google Scholar
Jaffe EK (2003) An unusual phylogenetic variation in the metal ion binding sites of porphobilinogen synthase. Chem Biol 10:25–34
Article
CAS
PubMed
Google Scholar
Jahn D, Verkamp E, Söll D (1992) Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis. Trends Biochem Sci 17:215–218
Article
CAS
PubMed
Google Scholar
Jordan PM (1994) The biosynthesis of uroporphyrinogen III: mechanism of action of porphobilinogen deaminase. In: The biosynthesis of tetrapyrrole pigments. Wiley, Chichester
Jordan PM, Warren MJ (1987) Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase. FEBS Lett 225:87–92
Article
CAS
PubMed
Google Scholar
Kikuchi G, Kumar AM, Tamalge P, Shemin D (1958) The enzymatic synthesis of δ-aminolevulinic acid. J Biol Chem 233:1214–1219
CAS
Google Scholar
Klemm DJ, Barton LL (1987) Purification and properties of protoporphyrinogen oxidase from an anaerobic bacterium, Desulfovibrio gigas. J Bacteriol 169:5209–5215
CAS
PubMed
Google Scholar
Laghai A, Jordan PM (1977) An exchange reaction catalysed by delta-aminolevulinate synthase from Rhodopseudomonas spheroides. Biochem Soc Trans 5:299–300
CAS
PubMed
Google Scholar
Layer G, Verfurth K, Mahlitz E, Jahn D (2002) Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli. J Biol Chem 277:34136–34142
Article
CAS
PubMed
Google Scholar
Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S (2000) Structural and mechanistic basis of porphyrin metallation by ferrochelatase. J Mol Biol 297:221–232
CAS
PubMed
Google Scholar
Lee HJ, Lee SB, Chung JS, Han SU, Han O, Guh JO, Jeon JS, An G, Back K (2000) Transgenic rice plants expressing a Bacillus subtilis protoporphyrinogen oxidase gene are resistant to diphenyl ether herbicide oxyfluorfen. Plant Cell Physiol 41:743–749
CAS
PubMed
Google Scholar
Luo J, Lim CK (1993) Order of uroporphyrinogen III decarboxylation on incubation of porphobilinogen and uroporphyrinogen III with erythrocyte uroporphyrinogen decarboxylase. Biochem J 289:529–532
CAS
PubMed
Google Scholar
Magnusson S, Ekstrom TJ, Elmer E, Kanje M, Ny L, Alm P (2000) Heme oxygenase-1, heme oxygenase-2 and biliverdin reductase in peripheral ganglia from rat, expression and plasticity. Neuroscience 95:821–829
Article
CAS
PubMed
Google Scholar
Malik Z, Lugaci H (1987) Destruction of erythroleukaemic cells by photoactivation of endogenous porphyrins. Br J Cancer 56:589–595
CAS
PubMed
Google Scholar
Martens JH, Barg H, Warren MJ, Jahn D (2002) Microbial production of vitamin B12. Appl Microbiol Biotechnol 58:275–285
Article
PubMed
Google Scholar
Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A (2001) Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism. J Biol Chem 276:44108–44116
Article
CAS
PubMed
Google Scholar
Mathews MA, Schubert HL, Whitby FG, Alexander KJ, Schadick K, Bergonia HA, Phillips JD, Hill CP (2001) Crystal structure of human uroporphyrinogen III synthase. EMBO J 20:5832–5839
Article
CAS
PubMed
Google Scholar
Medlock AE, Dailey HA (1996) Human coproporphyrinogen oxidase is not a metalloprotein. J Biol Chem 271:32507–32510
Article
CAS
PubMed
Google Scholar
Montforts FP, Glasenapp-Breiling M (2002) Naturally occurring cyclic tetrapyrroles. Fortschr Chem Org Naturst 84:1–51
CAS
PubMed
Google Scholar
Moser J, Lorenz S, Hubschwerlen C, Rompf A, Jahn D (1999) Methanopyrus kandleri glutamyl-tRNA reductase. J Biol Chem 274:30679–30685
CAS
PubMed
Google Scholar
Moser J, Schubert WD, Beier V, Bringemeier I, Jahn D, Heinz DW (2001) V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis. EMBO J 20:6583–6590
Article
CAS
PubMed
Google Scholar
Moser J, Schubert WD, Heinz DW, Jahn D (2002) Structure and function of glutamyl-tRNA reductase involved in 5-aminolaevulinic acid formation. Biochem Soc Trans 30:579–584
CAS
PubMed
Google Scholar
Nandi DL (1978) Studies on delta-aminolevulinic acid synthase of Rhodopseudomonas spheroides. Reversibility of the reaction, kinetic, spectral, and other studies related to the mechanism of action. J Biol Chem 253:8872–8877
CAS
PubMed
Google Scholar
O'Brian MR, Thöny-Meyer L (2002) Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes. Adv Microb Physiol 46:257–318
CAS
PubMed
Google Scholar
O'Neill GP, Söll D (1990) Transfer RNA and the formation of the heme and chlorophyll precursor, 5-aminolevulinic acid. Biofactors 2:227–235
CAS
PubMed
Google Scholar
Panek H, O'Brian MR (2002) A whole genome view of prokaryotic haem biosynthesis. Microbiology 148:2273–2282
CAS
PubMed
Google Scholar
Raux E, Leech HK, Beck R, Schubert HL, Santander PJ, Roessner CA, Scott AI, Martens JH, Jahn D, Thermes C, Rambach A, Warren MJ (2003) Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium. Biochem J 370:505–516
Article
CAS
PubMed
Google Scholar
Sasarman A, Chartrand P, Lavoie M, Tardif D, Proschek R, Lapointe C (1979) Mapping of a new hem gene in Escherichia coli K12. J Gen Microbiol 113:297–303
CAS
PubMed
Google Scholar
Sasarman A, Letowski J, Czaika G, Ramirez V, Nead MA, Jacobs JM, Morais R (1993) Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12. Can J Microbiol 39:1155–1161
CAS
PubMed
Google Scholar
Schauer S, Chaturvedi S, Randau L, Moser J, Kitabatake M, Lorenz S, Verkamp E, Schubert WD, Nakayashiki T, Murai M, Wall K, Thomann HU, Heinz DW, Inokuchi H, Söll D, Jahn D (2002) Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate. J Biol Chem 277:48657–48663
Article
CAS
PubMed
Google Scholar
Schauer S, Lüer C, Moser J (2003) Large scale production of biologically active Escherichia coli glutamyl-tRNA reductase from inclusion bodies. Protein Expr Purif (in press)
Schobert M, Jahn D (2002) Regulation of heme biosynthesis in non-phototrophic bacteria. J Mol Microbiol Biotechnol 4:287–294
CAS
PubMed
Google Scholar
Schubert HL, Raux E, Matthews MA, Phillips JD, Wilson KS, Hill CP, Warren MJ (2002a) Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase. Biochem Soc Trans 30:595–600
CAS
PubMed
Google Scholar
Schubert W-D, Moser J, Schauer S, Heinz DW, Jahn D (2002b) Structure and function of glutamyl-tRNA reductase, the first enzyme of tetrapyrrole biosynthesis in plants and prokaryotes. Photosynth Res 74:205–215
Article
CAS
Google Scholar
Shemin D, Russell CS (1953) Delta-aminolevulinic acid, its role in the biosynthesis of porphyrins and purines. J Am Chem Soc 75:4873–4875
CAS
Google Scholar
Shoolingin-Jordan PM, Spencer P, Sarwar M, Erskine PE, Cheung KM, Cooper JB, Norton EB (2002) 5-Aminolaevulinic acid dehydratase: metals, mutants and mechanism. Biochem Soc Trans 30:584–590
CAS
PubMed
Google Scholar
Shoolingin-Jordan PM, Al-Daihan S, Alexeev D, Baxter RL, Bottomley SS, Kahari ID, Roy I, Sarwar M, Sawyer L, Wang SF (2003) 5-Aminolevulinic acid synthase: mechanism, mutations and medicine. Biochim Biophys Acta 1647:361–366
Article
CAS
PubMed
Google Scholar
Sidler W (1994) Phycobilisomes and phycobiliprotein structure. In: Bryant DA (ed) The molecular biology of cyanobacteria. Kluwer, Dordrecht, pp 139–216
Smith MA, Grimm B, Kannangara CG, von Wettstein D (1991a) Spectral kinetics of glutamate-1-semialdehyde aminomutase of Synechococcus. Proc Natl Acad Sci USA 88:9775–9779
CAS
PubMed
Google Scholar
Smith MA, Kannangara CG, Grimm B, von Wettstein D (1991b) Characterization of glutamate-1-semialdehyde aminotransferase of Synechococcus. Steady-state kinetic analysis. Eur J Biochem 202:749–757
CAS
PubMed
Google Scholar
Smith MA, Kannangara CG, Grimm B (1992) Glutamate 1-semialdehyde aminotransferase: anomalous enantiomeric reaction and enzyme mechanism. Biochemistry 31:11249–11254
CAS
PubMed
Google Scholar
Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE (2001) Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 29:1097–1106
CAS
PubMed
Google Scholar
Thauer RK, Bonacker LG (1994) Biosynthesis of coenzyme F430, a nickel porphinoid involved in methanogenesis. Ciba Found Symp 180:210––227
CAS
PubMed
Google Scholar
Tyacke RJ, Contestabile R, Grimm B, Harwood JL, John RA (1995) Reactions of glutamate semialdehyde aminotransferase (glutamate-1-semialdehyde 2,1 aminomutase) with vinyl and acetylenic substrate analogues analysed by rapid scanning spectrophotometry. Biochem J 309:307–313
CAS
PubMed
Google Scholar
Vavilin DV, Vermaas WF (2002) Regulation of the tetrapyrrole biosynthetic pathway leading to heme and chlorophyll in plants and cyanobacteria. Physiol Plant 115:9–24
Article
CAS
PubMed
Google Scholar
Verneuil H de, Sassa S, Kappas A (1983) Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes. A single enzyme catalyzing the four sequential decarboxylations of uroporphyrinogens I and III. J Biol Chem 258:2454–2460
PubMed
Google Scholar
Warren MJ, Scott AI (1990) Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors. Trends Biochem Sci 15:486–491
Article
PubMed
Google Scholar
Weinstein JD, Beale SI (1983) Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis. J Biol Chem 258:6799–6807
CAS
PubMed
Google Scholar
Whitby FG, Phillips JD, Kushner JP, Hill CP (1998) Crystal structure of human uroporphyrinogen decarboxylase. EMBO J 17:2463–2471
Article
CAS
PubMed
Google Scholar
Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC (2001) The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat Struct Biol 8:156–160
CAS
PubMed
Google Scholar
Zumft WG (1997) Cell biology and molecular basis of denitrification. Microbiol Mol Biol Rev 61:533–616
CAS
PubMed
Google Scholar