Nucleotide sequence for the hemD gene of Escherichia coli encoding uroporphyrinogen III synthase and initial evidence for a hem operon

Jordan, Peter M.; Mgbeje, B I A; Thomas, Steven; Alwan, Asam F.

doi:10.1042/bj2490613

Cited by 45 publications

(19 citation statements)

References 21 publications

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“…( 25 and 21% identity to the sequence of UrolIl synthase from E. coli (1,26,48) and from humans (53), respectively (data not shown). The sequence identity between E. coli and human Urolll synthase is 20%.…”

Section: 1mentioning

confidence: 99%

“…This failure may reflect the low amount of hemA mRNA in the cells. In E. coli, hemC and hemD are closely linked and may form an operon (1,6,26,48), whereas hemA, hemB, and popC are located at different positions on the chromosome (6). Our present demonstration of a close linkage in B. subtilis between the genes encoding enzymes required for synthesis of UroIII from glutamyl-tRNA lends further support to the notion that genes encoding enzymes of a common biosynthetic pathway generally have a more compact organization in B. subtilis than in E. coli and other enteric bacteria (60).…”

Section: 1mentioning

confidence: 99%

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The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III

et al. 1991

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We have recently reported (M. Petricek, L. Rutberg, I. Schröder, and L. Hederstedt, J. Bacteriol. 172: 2250-2258, 1990) the cloning and sequence of a Bacillus subtilis chromosomal DNA fragment containing hemA proposed to encode the NAD(P)H-dependent glutamyl-tRNA reductase of the C5 pathway for 5-aminolevulinic acid (ALA) synthesis, hemX encoding a hydrophobic protein of unknown function, and hemC encoding hydroxymethylbilane synthase. In the present communication, we report the sequences and identities of three additional hem genes located immediately downstreatm of hemC, namely, hemD encoding uroporphyrinogen III synthase, hemB encoding porphobilinogen synthase, and hemL encoding glutamate-1-semialdehyde 2,1-aminotransferase. The six genes are proposed to constitute a hem operon encoding enzymes required for the synthesis of uroporphyrinogen III from glutamyl-tRNA. hemA, hemB, hemC, and hemD have all been shown to be essential for heme synthesis. However, deletion of an internal 427-bp fragment of hemL did not create a growth requirement for ALA or heme, indicating that formation of ALA from glutamate-1-semialdehyde can occur spontaneously in vivo or that this reaction may also be catalyzed by other enzymes. An analysis of B. subtilis carrying integrated plasmids or deletions-substitutions in or downstream of hemL indicates that no further genes in heme synthesis are part of the proposed hem operon.

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Section: 1mentioning

confidence: 99%

Section: 1mentioning

confidence: 99%

The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III

et al. 1991

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“…The might be hemH was sequenced in E. coli (44). The hem genes are all unlinked with the exception of the hemC and hemD genes, which have been suggested to form an operon (36,56). Virtually nothing is known about the regulation of heme biosynthesis.…”

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confidence: 99%

The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation

Delling

Elliott

1992

J Bacteriol

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Insertion mutagenesis has been used to isolate Salmonella typhimurium strains that are blocked in the conversion of 5-aminolevulinic acid (ALA) to heme. These mutants define the steps of the heme biosynthetic pathway after ALA. Insertions were recovered at five unlinked loci: hemB, hemCD, and hemE, which have been mapped previously in S. typhimurium, and hemG and hemH, which have been described only for Escherichia coli. No other simple hem mutants were found. However, double mutants are described that are auxotrophic for heme during aerobic growth and fail to convert coproporphyrinogen III to protoporphyrinogen IX. These mutant strains are defective in two genes, hemN and hemF. Single mutants defective only in hemN require heme for anaerobic growth on glycerol plus nitrate but not for aerobic growth on glycerol. Mutants defective only in hemF have no apparent growth defect. We suggest that these two genes encode alternative forms of coproporphyrinogen oxidase. Anaerobic heme synthesis requires hemN function, while either hemN or hemF is sufficient for aerobic heme synthesis. These phenotypes are consistent with the requirement of a well-characterized class of coproporphyrinogen oxidase for molecular oxygen.

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“…This reaction involves inversion of the D ring of HMBL and cyclization, with the release of one water molecule. In E. coli, cosynthetase is encoded by the hemD gene (10). The level of UP I was greatly elevated in the recombinant strains of P. freudenreichii that carried a hemA gene.…”

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confidence: 98%

Effects of Expression of hemA and hemB Genes on Production of Porphyrin in Propionibacterium freudenreichii

Piao

Kiatpapan

Yamashita

et al. 2004

Appl Environ Microbiol

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The genus Propionibacterium has a wide range of probiotic activities that are exploited in dairy and fermentation systems such as cheeses, propionic acid, and tetrapyrrole compounds. In order to improve production of tetrapyrrole compounds, we expressed the hemA gene, which encodes ␦-aminolevulinic acid (ALA) synthase from Rhodobacter sphaeroides, and the hemB gene, which encodes porphobilinogen (PBG) synthase from Propionibacterium freudenreichii subsp. shermanii IFO12424, either monocistronically or polycistronically in strain IFO12426. The recombinant strains accumulated larger amounts of ALA and PBG, with resultant 28-to 33-fold-higher production of porphyrinogens, such as uroporphyrinogen and coproporphyrinogen, than those observed in strain IFO12426, which harbored the shuttle vector pPK705.

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Nucleotide sequence for the hemD gene of Escherichia coli encoding uroporphyrinogen III synthase and initial evidence for a hem operon

Cited by 45 publications

References 21 publications

The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III

The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III

The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation

Effects of Expression of hemA and hemB Genes on Production of Porphyrin in Propionibacterium freudenreichii

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