Studies on the biosynthesis of bialaphos (SF-1293). 9. Biochemical mechanism of C-P bond formation in bialaphos: Discovery of phosphoenolpyruvate phosphomutase which catalyzes the formation of phosphonopyruvate from phosphoenolpyruvete.

Hidaka, Tomomi; Mori, Michiko; Imai, Shoichi; Hara, Osamu; Nagaoka, Kozo; Seto, Haruo

doi:10.7164/antibiotics.42.491

Cited by 51 publications

(44 citation statements)

References 17 publications

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“…Attempts to detect the forward reaction catalyzed by PEPPMwere unsuccessful based on the method using NADH/malate dehydrogenase. 4) This result supports the observation that the forward reaction is weaker than the reverse reaction, in agreement with the nature of PEPPMfrom S. hygroscopicus. Although PEPPMwas purified from Tetrahymena pyriformis and S. hygroscopicus, this is the first time of the detection of PEPPM activity in Gram-negative bacteria.…”

Section: Production Of C-p Compounds By Strain B-l and L-bsupporting

confidence: 80%

“…Recently phosphoenolpyruvate phosphomutase (PEPPM) catalyzing the C-P bond forming reaction was purified from Tetrahymena pyriformis3) and Streptomyces hygroscopicus, 4) and subsequently and surprisingly, the enzyme turned out to show stronger activity in catalyzing the reverse reaction, i.e., cleaving the C-P bond to give PEP, than the C-P bond formation. Although several studies on the mechanism of this reaction using PEPPMfrom Tetrahymena5) were reported, the detailed mechanism is still unclear.…”

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confidence: 99%

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A New Screening Method for C-P Compound Producing Organisms by the Use of Phosphoenolpyruvate Phosphomutase.

Nakashita

Shimazu

Seto

1991

Agricultural and Biological Chemistry

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Phosphoenolpyruvate phosphomutase (PEPPM)catalyzes the C-P bond forming reaction by intramolecular rearrangement of phosphoenolpyruvate to phosphonopyruvate, and shows stronger activity in catalyzing the reverse reaction than the forward reaction. By exploiting the activity of PEPPMto catalyze the reverse reaction, 81 strains were screened as possible C-P compoundproducing microorganisms from 230 soil samples. Twoof these strains, B-l and L-b, were found to produce C-P compounds by 31P-NMRspectral analysis of their broth filtrates.The activity of PEPPMwas detected in the cell extracts of these two strains. The strain B-l was identified as Pseudomonas gladioli, and hydroxyethylphosphonic acid (HEP) was isolated from the broth filtrate of this strain as a C-P compound.

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Section: Production Of C-p Compounds By Strain B-l and L-bsupporting

confidence: 80%

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confidence: 99%

A New Screening Method for C-P Compound Producing Organisms by the Use of Phosphoenolpyruvate Phosphomutase.

Nakashita

Shimazu

Seto

1991

Agricultural and Biological Chemistry

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“…The chemical strategy that we have seen unfold thus far involves intramolecular oxygen to carbon phosphoryl transfer in vinyl phosphate esters. This chemistry is exemplified by the catalysis of PEP mutase and its close relative, CPEP mutase (Hidaka et al, 1989). This paper describes the kinetics and mechanism of catalysis of P-C bond formation by the PEP mutase of Tetrahymena pyriformis.…”

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confidence: 99%

“…The study of phosphonate metabolism (Horiguchi, 1972;Barry et al, 1988;Seto et al, 1991;Hidaka et al, 1992Hidaka et al, , 1989Hammerschmidt, 1991;Kuzuyama et al, 1992;Seto, 1986;Hara et al, 1991;Kamigiri et al, 1992) is a relatively new field for which there is a rapidly growing interest. The synthesis of phosphonates relies on phosphate precursors and on enzyme mediated chemistry which converts the P-O bond to the P-C bond.…”

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confidence: 99%

“…This paper describes the kinetics and mechanism of catalysis of P-C bond formation by the PEP mutase of Tetrahymena pyriformis. First isolated from this protozoan Seidel et al, 1988), PEP mutase has since been purified from bacteria (Hidaka et al, 1989 and salt water mussel (Kim, 1994). In ViVo, the mutase functions in the synthesis of P-pyr, the first of three reactions leading from PEP to AEP (Scheme 1).…”

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Phosphoenolpyruvate Mutase Catalysis of Phosphoryl Transfer in Phosphoenolpyruvate: Kinetics and Mechanism of Phosphorus−Carbon Bond Formation

Kim

Dunaway‐Mariano

1996

Biochemistry

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Phosphoenolpyruvate phosphomutase (PEP mutase) from Tetrahymena pyriformis catalyzes the rearrangement of phosphoenolpyruvate (PEP) to phosphonopyruvate (P-pyr). A spectrophotometric P-pyr assay consisting of the coupled actions of P-pyr decarboxylase, phosphonoacetaldehyde hydrolase, and alcohol dehydrogenase was devised to monitor mutase catalysis. The reaction constants determined for PEP mutase catalyzed conversion of PEP to P-pyr at pH 7.5 and 25°C in the presence of Mg(II) are k cat ) 5 s -1 , K m ) 0.77 ( 0.05 mM, and K eq ) (2-9) × 10 -4 . In the PEP forming direction, k cat ) 100 s -1 and K m ) 3.5 ( 0.1 µM. P]phosphoenzyme-oxalate complex. In contrast, the same reaction carried out with pyruvate phosphate dikinase (PPDK), an enzyme known to catalyze the phosphorylation of its active site histidine with PEP, occurred at a rate of 4 × 10 -4 s -1 (15% E-P formed) in the presence Mg(II) and at a rate of 3 × 10 -3 s -1 (60% E-P formed) in the presence of Mn(II). Both oxalyl phosphate (K i ) 180 ( 10 µM) and oxalate (K i ) 32 ( 10 µM) were competitive inhibitors of PEP mutase catalysis, but neither displayed slow, tight binding inhibition. These results do not support the intermediacy of a phosphoenzyme-pyruvyl enolate complex in PEP mutase catalysis.

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Peptides

Wise

2000

Kirk-Othmer Encyclopedia of Chemical Technology

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Peptide antibiotics are classified according to their overall shape, which can be linear or cyclic, and by the nature of the bonds joining the constituent amino acids and other carboxylic acids, which can be all amide bonds or amide plus ester bonds. Most peptide antibiotics are cyclic peptides that do not contain disulfide linkages. Peptide antibiotics differ in many respects from proteins. The vast majority of peptide antibiotics have molecular weights in the 500–1500 range, whereas the average protein has a mol wt of 40,000. Many peptide antibiotics have unusual fatty acids and amino acids, such as D ‐amino acids, N ‐methyl amino acids, or imino acids, and they usually lack methionine and histidine. Ring closure in cyclic peptide antibiotics is by amide or ester bonds. Peptide antibiotics are normally resistant to the usual proteases and peptidases. They are usually synthesized on multienzyme complexes much as are fatty acids, and not on ribosomes as are proteins. Most peptide antibiotics are synthesized as groups of closely related structures. Even the small fraction of peptide antibiotics that have therapeutic usefulness are quite toxic. The ratio of the minimum toxic dose to the maximum effective dose is smaller than for most nonpeptide antibiotics. Peptide antibiotics are not often the drugs of first choice for systemic therapy of important human disease. However, the World Health Organization, which chooses drugs especially for Third World use based on efficacy, safety, quality, price, and availability, includes such peptide antibiotics as bleomycin, dactinomycin, and bacitracin, plus several β‐lactams. The complex structure of peptide antibiotics adds considerably to the problems of synthesis, but more recent efforts toward improved peptide antibiotics are encouraging.

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Studies on the biosynthesis of bialaphos (SF-1293). 9. Biochemical mechanism of C-P bond formation in bialaphos: Discovery of phosphoenolpyruvate phosphomutase which catalyzes the formation of phosphonopyruvate from phosphoenolpyruvete.

Cited by 51 publications

References 17 publications

A New Screening Method for C-P Compound Producing Organisms by the Use of Phosphoenolpyruvate Phosphomutase.

A New Screening Method for C-P Compound Producing Organisms by the Use of Phosphoenolpyruvate Phosphomutase.

Phosphoenolpyruvate Mutase Catalysis of Phosphoryl Transfer in Phosphoenolpyruvate: Kinetics and Mechanism of Phosphorus−Carbon Bond Formation

Peptides

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