Proof by synthesis that unrearranged hydroxymethylbilane is the product from deaminase and the substrate for cosynthetase in the biosynthesis of uro'gen-III

Battersby, Alan R.; Fookes, Christopher J. R.; Gustafson-Potter, Kerstin E.; Matcham, George W. J.; McDonald, Edward

doi:10.1039/c39790001155

Cited by 68 publications

(32 citation statements)

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“…Free HMB spontaneously cyclizes to form the nonphysiological product Urogen I, in which the D ring is conjugated with the A ring in the reverse orientation (Battersby et al 1979). Therefore, the presence of UROS is essential for the synthesis of tetrapyrroles.…”

Section: Urogen III Synthasementioning

confidence: 99%

Tetrapyrrole Metabolism inArabidopsis thaliana

Tanaka

Kobayashi²,

Masuda

2011

The Arabidopsis Book

226

232

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This manuscript is dedicated to Prof. Mamoru Mimuro of Kyoto University who passed away in Februay 2011.Higher plants produce four classes of tetrapyrroles, namely, chlorophyll (Chl), heme, siroheme, and phytochromobilin. In plants, tetrapyrroles play essential roles in a wide range of biological activities including photosynthesis, respiration and the assimilation of nitrogen/sulfur. All four classes of tetrapyrroles are derived from a common biosynthetic pathway that resides in the plastid. In this article, we present an overview of tetrapyrrole metabolism in Arabidopsis and other higher plants, and we describe all identified enzymatic steps involved in this metabolism. We also summarize recent findings on Chl biosynthesis and Chl breakdown. Recent advances in this field, in particular those on the genetic and biochemical analyses of novel enzymes, prompted us to redraw the tetrapyrrole metabolic pathways. In addition, we also summarize our current understanding on the regulatory mechanisms governing tetrapyrrole metabolism. The interactions of tetrapyrrole biosynthesis and other cellular processes including the plastid-to-nucleus signal transduction are discussed.

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Section: Urogen III Synthasementioning

confidence: 99%

Tetrapyrrole Metabolism inArabidopsis thaliana

Tanaka

Kobayashi²,

Masuda

2011

The Arabidopsis Book

226

232

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“…The hemD gene encodes for the uroporphyrinogen-III cosynthase (E.C. 4.2.1.75), the enzyme responsible for the conversion of hydroxymethylbilane to uroporphyrinogen III (3,12). The latter represents the last common intermediate of the three pathways, i.e., the heme, chlorophyll, and corin pathways.…”

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confidence: 99%

Molecular cloning and sequencing of the hemD gene of Escherichia coli K-12 and preliminary data on the Uro operon

Săsárman¹,

Nepveu²,

Echelard³

et al. 1987

J Bacteriol

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DNA of plasmid pSAS1002TH (F' ilv+ hemD+ hemC+ cya+) was used to clone the hemD gene of Escherichia coli K-12. Due to poor transformability of the heme-deficient mutants, the restriction fragments of the F' plasmid were first cloned into a mobilizable derivative of pBR322, pSAS1211LP, which was then mobilized into a hemD recA mutant (E. coli SASX419AN). One recombinant plasmid, carrying a HindIII fragment of about 5 kilobases (kb), was shown to complement the hemD mutant and also a cya mutant of E. coli K-12, as well as a hemC mutant of Salmonella typhimurium LT2. Further subcloning of the insert enabled us to locate the hemD gene to a BamHI-PstI fragment (approximately 2.3 kb) which also carried the hemC gene. The hemD gene occupies a region close to the PstI end, since the deletion of a 0.6-kb fragment from this end resulted in loss of the ability to complement the hemD mutation. The use of the promoter-probe vector pK01 and the results of complementation showed that the hemD gene was transcribed under physiological conditions from the same promoter as the hemC gene, the direction of transcription being hemC-hemD. This allows us to define a new polycistronic operon of E. coli K-12, for which we propose the designation Uro operon. Sequencing of the hemD gene showed the presence of an open reading frame (ORF) of 738 nucleotides which could code for a protein with a molecular weight of 27,766, which should correspond to the hemD protein; the ORF starts with the last nucleotide of the hemC gene, the two genes having different reading frames. An ORF of at least 480 base pairs follows the hemD gene after a few nucleotides. The corresponding gene X, the function of which is unknown, might represent a third member of the Uro operon.

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“…Intriguingly, this enzyme utilizes a dipyrromethane primer as a cofactor and thus in fact, first generates a hexapyrrolic species which then is cleaved to hydroxymethylbilane [120][121][122][123]. In a sense this bilane is a symmetric arrangement of four pyrroles and can spontaneously cyclize to the symmetric uroporphyrinogen I [124]. Under enzymatic control a desymmetrization occurs whereby uroporphyrinogen III synthase cyclizes and isomerizes hydroxymethylbilane to the spiro intermediate 41 under inversion of ring D [120,125,126] which then yields uroporphyrinogen III 2.…”

Section: Formation Of Protoporphyrin IXmentioning

confidence: 99%

Chlorophylls, Symmetry, Chirality, and Photosynthesis

et al. 2014

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Chlorophylls are a fundamental class of tetrapyrroles and function as the central reaction center, accessory and photoprotective pigments in photosynthesis. Their unique individual photochemical properties are a consequence of the tetrapyrrole macrocycle, the structural chemistry and coordination behavior of the phytochlorin system, and specific substituent pattern. They achieve their full potential in solar energy conversion by working in concert in highly complex, supramolecular structures such as the reaction centers and light-harvesting complexes of photobiology. The biochemical function of these structures depends on the controlled interplay of structural and functional principles of the apoprotein and pigment cofactors. Chlorophylls and bacteriochlorophylls are optically active molecules with several chiral centers, which are necessary for their natural biological function and the assembly of their supramolecular complexes. However, in many cases the exact role of chromophore stereochemistry in the biological context is unknown. This review gives an overview of chlorophyll research in terms of basic function, biosynthesis and their functional and structural role in photosynthesis. It highlights aspects of chirality and symmetry of chlorophylls to elicit further interest in their role in nature.

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Proof by synthesis that unrearranged hydroxymethylbilane is the product from deaminase and the substrate for cosynthetase in the biosynthesis of uro'gen-III

Cited by 68 publications

References 0 publications

Tetrapyrrole Metabolism inArabidopsis thaliana

Tetrapyrrole Metabolism inArabidopsis thaliana

Molecular cloning and sequencing of the hemD gene of Escherichia coli K-12 and preliminary data on the Uro operon

Chlorophylls, Symmetry, Chirality, and Photosynthesis

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