Biosynthesis of porphyrins and related macrocycles. Part 20. Purification of deaminase and studies on its mode of action

Battersby, Alan R.; Fookes, Christopher J. R.; Matcham, George W. J.; McDonald, Edward; Hollenstein, Roger

doi:10.1039/p19830003031

Cited by 45 publications

(18 citation statements)

References 8 publications

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“…Euglena gracilis was maintained in liquid culture in the light as described previously [12]. For enzyme preparations and extraction of RNA, cells were harvested after four days.…”

Section: Growth Of Euglena Gracilismentioning

confidence: 99%

“…Production of antibodies, Western blot analysis and determination of the N-terminal amino acid sequence Euglena hydroxymethylbilane synthase, purified to homogeneity as described by Battersby et a1 [12], was a gift of Dr G. J. Hart.…”

Section: Growth Of Euglena Gracilismentioning

confidence: 99%

“…Euglena hydroxymethylbilane synthase has been purified to homogeneity [12] and characterised extensively in kinetic and active site studies [13, 141. Interestingly, the Euglena chloroplast differs from that in higher plants and green algae in that it has three, not two, outer membranes [15]. The origin of this extra membrane remains uncertain, but it is possible that the structure of the transit peptide of nuclear-encoded chloroplast proteins may provide some clues.…”

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confidence: 99%

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Isolation and characterisation of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis

Sharif

Smith

Abell³

1989

European Journal of Biochemistry

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A cDNA expression library was constructed from light‐grown Euglena gracilis poly(A)‐rich RNA in λgt11. Antibodies to Euglena hydroxymethylbilane synthase, the third enzyme in the porphyrin biosynthetic pathway, were used to screen the library and a clone encoding part of the sequence of hydroxymethylbilane synthase was identified. This was used to rescreen the library and a full‐length clone was isolated, which encoded not only the entire mature protein (Mr 36 927), but also an N‐terminal extension of 139 amino acids. The deduced Mr of the whole polypeptide is 51 744, which corresponds to the size of the protein immunoprecipitated from the translation products of Euglena poly(A)‐rich RNA. The mature protein is 60–70% similar to hydroxymethylbilane synthase from human erythrocytes and Escherichia coli. The sequence of the N‐terminal extension has similarities to both the transit peptides of chloroplast proteins and those for the endoplasmic reticulum. This is the first report both of a cDNA clone for an enzyme of the chlorophyll biosynthetic pathway and of a putative transit peptide for a nuclear‐encoded Euglena protein.

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“…Euglena gracilis was maintained in liquid culture in the light as described previously [12]. For enzyme preparations and extraction of RNA, cells were harvested after four days.…”

Section: Growth Of Euglena Gracilismentioning

confidence: 99%

Section: Growth Of Euglena Gracilismentioning

confidence: 99%

mentioning

confidence: 99%

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Isolation and characterisation of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis

Sharif

Smith

Abell³

1989

European Journal of Biochemistry

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“…Chlorophyll was estimated by the method of Arnon (18) and PBGD activity was assayed essentially as described (10). Protein was determined with the Bio-Rad protein assay.…”

mentioning

confidence: 99%

“…In our laboratory, we have isolated a Euglena cDNA clone for one of these enzymes, porphobilinogen deaminase (PBGD, also known as hydroxymethylbilane synthase: EC 4.3.1.8) (9) by using antibodies raised against the enzyme purified from light-grown Euglena (10). This clone encodes the mature protein and an N-terminal extension of 139 amino acids, which has the characteristics of a chloroplast transit peptide, so the protein is presumably located in the chloroplast.…”

mentioning

confidence: 99%

Expression and subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in light-grown Euglena gracilis and three nonchlorophyllous cell lines.

Shashidhara

Smith

1991

Proc. Natl. Acad. Sci. U.S.A.

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The Evidence for a Spirocyclic Intermediate in the Formation of Uroporphyrinogen III by Cosynthase

Leeper

2007

Ciba Foundation Symposium 180 ‐ the Biosynthesis of the Tetrapyrrole Pigments

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Biosynthesis of porphyrins and related macrocycles. Part 20. Purification of deaminase and studies on its mode of action

Cited by 45 publications

References 8 publications

Isolation and characterisation of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis

Isolation and characterisation of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis

Expression and subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in light-grown Euglena gracilis and three nonchlorophyllous cell lines.

The Evidence for a Spirocyclic Intermediate in the Formation of Uroporphyrinogen III by Cosynthase

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