Inhibition of tyrosine-sensitive 3-deoxy-?-arabino-heptulosonate 7-phosphate synthase by glyphosate in Candida maltosa

Bode, R

doi:10.1016/0378-1097(84)90063-6

Cited by 3 publications

(5 citation statements)

References 9 publications

(11 reference statements)

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“…(Bode andBirnbaum 1984, 1991c;Bode et al 1984aLippoldt et al 1986). Candida maltosa synthesizes phenylalanine and tyrosine only via phenylpyruvate and p-hydroxyphenylpyruvate, respectively, using the enzymes chorismate mutase (EC 5.4.99.5), prephenate dehydratase (EC 4.2.1.51), and prephenate dehydrogenase (EC 1.3.1.12 or 13), whereas the arogenate pathway is not active in this yeast (Bode and Birnbaum 1984;Bode et al 1984cBode et al , 1985d.…”

Section: Amino Acid Biosynthesismentioning

confidence: 97%

“…Glyphosate Action in C. maltosa (Bode et al 1984a(Bode et al ,b,d, 1985bBode and Birnbaum 1989). The broad-spectrum herbicide glyphosate (N [posphonomethyl]-glycine) was studied as an inhibitor of enzymes involved in the shikimate pathway, representing the first steps, finally leading to chorismate, in biosynthesis of aromatic amino acids in C. maltosa.…”

Section: Biosynthesis Of Aromatic Amino Acidsmentioning

confidence: 99%

“…The amount of aromatic amino acids in the free amino acid pool of C. maltosa cells indicates that the biosynthesis of phenylalanine and tyrosine can be regulated only by tryptophan. The regulation of tryptophan concentration is affected by the inhibition of anthranilate synthase by tryptophan, whereas the common branch of the biosynthesis of aromatic compounds is controlled by two isozymic tyrosine-sensitive and a phenylalanine-sensitive 3-deoxy-Darabinoheptulosonic acid 7-phosphate (DAHP) synthases, constitutive enzymes catalyzing the first step in the biosynthesis of aromatic amino acids (Bode et al 1984a(Bode et al , 1985c.…”

Section: Amino Acid Biosynthesismentioning

confidence: 99%

See 2 more Smart Citations

Candida maltosa

Mauersberger

Ohkuma

Schunck

et al. 1996

Nonconventional Yeasts in Biotechnology

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Section: Amino Acid Biosynthesismentioning

confidence: 97%

Section: Biosynthesis Of Aromatic Amino Acidsmentioning

confidence: 99%

Section: Amino Acid Biosynthesismentioning

confidence: 99%

See 1 more Smart Citation

Candida maltosa

Mauersberger

Ohkuma

Schunck

et al. 1996

Nonconventional Yeasts in Biotechnology

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“…The DAHP synthase catalyzes the condensation of PEP and erythrose-4-phosphate (E4P) to 3-deoxy- d -arabino-heptulosonate 7-phosphate (DAHP), which is the initial reaction of the aromatic amino acid biosynthetic pathway. However, two DAHP synthase isozymes from other organisms were inhibited at 1 mM glyphosate and explained by competitive substrate inhibition: one in mung bean in competition with E4P (Rubin et al ( 1982 ) and the other one in the yeast Candida maltosa in competition with PEP (Bode et al 1984 ). Both organisms have insensitive DAHP synthase isoenzymes as well.…”

Section: Modes Of Action Of Glyphosatementioning

confidence: 99%

Glyphosate, a chelating agent—relevant for ecological risk assessment?

Mertens

Höss

Neumann

et al. 2018

Environ Sci Pollut Res

155

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Glyphosate-based herbicides (GBHs), consisting of glyphosate and formulants, are the most frequently applied herbicides worldwide. The declared active ingredient glyphosate does not only inhibit the EPSPS but is also a chelating agent that binds macro- and micronutrients, essential for many plant processes and pathogen resistance. GBH treatment may thus impede uptake and availability of macro- and micronutrients in plants. The present study investigated whether this characteristic of glyphosate could contribute to adverse effects of GBH application in the environment and to human health. According to the results, it has not been fully elucidated whether the chelating activity of glyphosate contributes to the toxic effects on plants and potentially on plant–microorganism interactions, e.g., nitrogen fixation of leguminous plants. It is also still open whether the chelating property of glyphosate is involved in the toxic effects on organisms other than plants, described in many papers. By changing the availability of essential as well as toxic metals that are bound to soil particles, the herbicide might also impact soil life, although the occurrence of natural chelators with considerably higher chelating potentials makes an additional impact of glyphosate for most metals less likely. Further research should elucidate the role of glyphosate (and GBH) as a chelator, in particular, as this is a non-specific property potentially affecting many organisms and processes. In the process of reevaluation of glyphosate its chelating activity has hardly been discussed.

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“…We have recently shown that the first reaction of the branched aromatic pathway in the n-alkane utilising yeast Candida maltosa is also catalysed by two isozymes (BODE et al 1984a). In the present paper we describe some catalytic properties of these isozymes and report that the DAHP synthases are not only inhibited by phenylalanine or tyrosine but also by intermediates and analogues.…”

mentioning

confidence: 99%

Regulatory properties of 3‐deoxy‐D‐arabino‐heptulosonate‐7‐phosphate synthase isozymes from Candida maltosa

Bode

Melo

Birnbaum

1985

J. Basic Microbiol.

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The first step in the biosynthesis of aromatic amino acids by Candida maltosa was eatalysed by two isozymes of 3-deoxy-~-arabino-heptulosonate 7-phosphate (DAHP) synthase. The formation of which was constitutive. The phenylalanine-sensitive and the tyrosine-sensitive DAHP synthases were partially purified by hydroxylapatite chromatography and several properties of the separated isozymes were studied. Both enzymes showed a molecular weight of 90,000. The Km-values of the tyrosine-sensitive DAHP synthase were 0.20 mM for erythrose-4-phosphate (E-4-P) and 0.50 mm for phosphoenolpyruvate (PEP). Inhibition of this isozyme reaction by L-tyrosine was competitive with respect to E-4-P (Ki = 0.028 mM) and non-competitive with respect to PEP.The Km-values of the phenylalanine-sensitive DAHP synthase were estimated to be 0.85 mM for E-4-P and 0.63 mm for PEP; a Ki of 0.097 mix was obtained for L-phenylalanine. A number of tyrosine and phenylalanine analogues and biosynthetic intermediates also inhibited the two isozyme reactions. For example, we observed a strong inhibitory effect of p-hydroxyphenylpyruvate on the tyrosine-sensitive DAHP synthase and of phenylpyruvate on the phenylalanine-sensitive isozyme. Prephenate and arogenate had a less pronounced effect on the phenylalanine-sensitive DAHP synthase.In microorganisms and plants 3-deoxy-~-arabino-hcptulosonate 7-phosphate synthase (DAHP synthase) catalyses the first reaction of the common biosynthesis pathway for aromatic amino acids. The mechanisms of regulation of the enzyme have been studied in a wide variety of organisms. it has been shown that DAHP synthase is a regulated enzyme that is subject to the most diverse number of distinctly different patterns of feedback inhibition known for a single enzyme (JENSEN and REBELLO 1970). These properties of DAHP synthase exist in nature to regulate the multibranched pathway of aromatic biosynthesis and ensure an unimpaired formation of all endproducts.I n Neurospora crassa and enterobacteria three isozymes of DAHP synthase have been described which are feedback inhibited by phenylalanine, tyrosine or tryptophan ( BROWN and DOY 1966, JENSEN andNASSER 1968). In contrast, in cyanobacteria, Euglena and some species of PsedomoncLs the enzyme is a single protein, which can be inhibited by one or more aromatic amino acids (HALL et al. , BYNG et al. 1981, WIIITAKER et al. 1981. Two isozymes exist in the three yeast species Saccharomyces cerevisiae, Schizosaccharomyces pombe and Hansenula henricii, examined so far : a tyrosine-sensitive and a phenylalanine-sensitive DAHP synthase (LINGENS et , SCHWEINGRUBER and WYSSLING 1974, BODE and BIRNBAUM 1978.We have recently shown that the first reaction of the branched aromatic pathway in the n-alkane utilising yeast Candida maltosa is also catalysed by two isozymes (BODE et al. 1984a). In the present paper we describe some catalytic properties of these isozymes and report that the DAHP synthases are not only inhibited by phenylalanine or tyrosine but also by intermediates and analogues.1 .

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Inhibition of tyrosine-sensitive 3-deoxy-?-arabino-heptulosonate 7-phosphate synthase by glyphosate in Candida maltosa

Cited by 3 publications

References 9 publications

Candida maltosa

Candida maltosa

Glyphosate, a chelating agent—relevant for ecological risk assessment?

Regulatory properties of 3‐deoxy‐D‐arabino‐heptulosonate‐7‐phosphate synthase isozymes from Candida maltosa

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