Interaction of ribulose bisphosphate carboxylase/oxygenase with 2-carboxyhexitol 1,6-bisphosphates

Roach, Daniel J. W.; Gollnick, Paul; Fadden, Bruce A. Mc

doi:10.1016/0003-9861(83)90505-2

Cited by 9 publications

(10 citation statements)

References 25 publications

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“…One day after chromatography, the lactone content of peaks I and II was less than 13% whereas pooled fractions representing peaks III and IV were predominantly lactones. This apparently anomalous sequence of elution in which the carboxytates are eluted from Dowex-1 earlier than the lactones confirms earlier results with the bisphosphates [11,12]. In contrast to the relatively clean chromatographic separation of the reaction mixture ( Figure 2) which had been incubated at a pH of 7.5, analogous workup and chromatography of the reaction mixture after condensation at a pH of 11.5 resulted in very poor separation of products.…”

Section: The Eyanohydrin Synthesis On F6psupporting

confidence: 86%

“…The ratio of these half-times is in basic agreement with that observed for the identical dephosphorylated lactones derived from the bisphosphates [12]. Accordingly, the compounds in peaks III and IV were the lactones of 2-C-carboxy-D-glucitol 6-phosphate (CG6P) and 2-Ccarboxy-D-mannitol 6-phosphate (CM6P), respectively ( Figure 3).…”

Section: The Eyanohydrin Synthesis On F6psupporting

confidence: 83%

“…In earlier research, the lactones of the corresponding 1,6-bisphosphates were also dephosphorylated with acid phosphatase (erroneously reported to be alkaline phosphatase, ref. 12 Figure 3. Structures of the lactones derived from peaks III and IV arising from the cyanohydrin synthesis on F6P (top row) and from peaks III and IV arising from the cyanohydrin synthesis on fructose-l-phosphate (F1P) (bottom row).…”

Section: The Eyanohydrin Synthesis On F6pmentioning

confidence: 99%

“…The cyanohydrin synthesis has been used to prepare 2-carboxyhexitol bisphosphates from frutose 1,6-bisphosphate [6,12]. The two products which are 1,6-bisphosphates of 2-C-carboxy-D-glucitol (CGBP) and 2-Ccarboxy-D-mannitol (CMBP), are excellent inhibitors [12] of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO), a key enzyme contributing both to photosynthesis and photorespiration [9].…”

Section: Introductionmentioning

confidence: 99%

“…The two products which are 1,6-bisphosphates of 2-C-carboxy-D-glucitol (CGBP) and 2-Ccarboxy-D-mannitol (CMBP), are excellent inhibitors [12] of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO), a key enzyme contributing both to photosynthesis and photorespiration [9]. The bisphosphates in the 2-carboxypentitol series have been analogously prepared from RuBP leading to the recognition that one, 2-C-carboxy-D-arabinitol inhibits barley growth when applied topically to leafy tissue or administered to the roots (unpublished observation, B.A.…”

Section: Introductionmentioning

confidence: 99%

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The inhibition of ribulose 1,5-bisphosphate carboxylase oxygenase by several 2-carboxyhexitol 1- and 6-phosphates

1986

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The condensation of D-fructose 6-phosphate or 1-phosphate with cyanide has been used to synthesize 2-carboxyhexitol 6-phosphates and 1-phosphates. The products have been characterized in terms of their action on ribulose bisphosphate carboxylase/oxygenase. The reaction of D-fructose 6-phosphate with cyanide is four times as fast (at 22°C) at pH 7.5 than at pH 11.5 and the primary products of condensation are more easily isolated by anion exchange chromatography. Two minor chromatographic peaks (I and II) for diastereomeric 2-carboxyhexitol 6-phosphates are isolated in addition to two major peaks, III and IV, which are lactones. The lactones are those of 2-C-carboxy-D-glucitol 6-phosphate (CG6P) in peak III and 2-C-carboxy-D-mannitol 6-phosphate (CM6P) in peak IV, as established after dephosphorylation by the relative rates of oxidation by periodate and by gas chromatographic retention times of the acetates. Analogous methodology has been used to synthesize the diastereomeric 2-carboxy-hexitol 1-phosphates (CG1P and CM1P) and their lactones from D-fructose 1-phosphate. The four carboxylates inhibit ribulose bisphosphate carboxylase/oxygenase from spinach or Pseudomonas oxalaticus in the following decreasing order of potency: CG6P, CM6P, CG1P, CM1P. The inhibition pattern suggests that the binding of the 5-phosphate moiety of the intermediate in the reaction catalyzed by ribulose bisphosphate carboxylase/oxygenase may be stronger by an order of magnitude than the binding of the 1-phosphate group.

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Section: The Eyanohydrin Synthesis On F6psupporting

confidence: 86%

Section: The Eyanohydrin Synthesis On F6psupporting

confidence: 83%

Section: The Eyanohydrin Synthesis On F6pmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The inhibition of ribulose 1,5-bisphosphate carboxylase oxygenase by several 2-carboxyhexitol 1- and 6-phosphates

1986

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Active-site histidines in recombinant cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase examined by site-directed mutagenesis

Haining

McFadden

1994

Photosynth Res

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The functions of His(291), His(295) and His(324) at the active-site of recombinant A. nidulans ribulose-1,5-bisphosphate carboxylase/ oxygenase have been explored by site-directed mutagenesis. Replacement of His(291) by K or R resulted in unassembled proteins, while its replacement by E, Q or N resulted in assembled but inactive proteins. These results are in accord with a metal ion-binding role of this residue in the activated ternary complex by analogy to x-ray crystallographic analyses of tobacco and spinach enzymes.His(324) (H327 in spinach), which is located within bonding distance of the 5-phosphate of bound bi-substrate analog 2-carboxyarabinitol 1,5-bisphosphate in the crystal structures, has been substituted by A, K, R, Q and N. Again with the exception of the H324K and R variants, these changes resulted in detectable assembled protein. The mutant H324A protein exhibited no detectable carboxylase activity, whereas the H324Q and H324N changes resulted in purifiable holoenzyme with 2.0 and 0.1% of the recombinant wild-type specific carboxylase activity, respectively. These results are consistent with a phosphate binding role for this residue.The replacement of His(295), which has been suggested to aid in phosphate binding, with Ala in the A. nidulans enzyme leads to a mutant with 5.8% of the recombinant wild-type carboxylase activity. All other mutations at this position resulted in unassembled proteins. Purified H295A and H324Q enzymes had elevated Km(RuBP) values and unchanged CO2/O2 specificity factors compared to recombinant wild-type.

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The response to ribulose bisphosphate4? (RuBP4?) and RuBP-Mg2? in catalysis by structurally divergent RuBP carboxylase/oxygenases

Roach

McFadden

1983

Photosynth Res

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Free ribulose hisphosphate (RuBP(4-)) rather than its magnesium complex (RuBP-Mg(2-)) was the apparent substrate for spinach ribulose bisphosphate carboxylase/oxygenase. The apparent Km for total RuBP (pH 8.0 at 30° C) increased with increasing Mg(2+) concentrations from 11.6 μM at 13.33 mM Mg(2+) to 32.6 μM at 40.33 mM Mg(2+). Similarly the apparent Km for RuBP-Mg(2-) complex increased with increasing Mg(2+) from 9.4 μM at 13.33 mM Mg(2+) to 29.7 μM at 40.33 mM Mg(2+). However, the Km values for uncomplexed RuBP(4-) were independent of the (saturating) concentration of Mg(2+) (Km=2.2 μM). The Vmax did not vary with the changing concentrations of Mg(2+).In contrast, the Km for total RuBP remained constant with varying Mg(2+) concentrations (Km=59.5 μM) for the enzyme from R. rubrum. The apparent Km for the RuBP-Mg(2-) complex decreased with increasing Mg(2+) concentrations from 16.0 μM at 7.5 mM Mg(2+) to 5.9 μM at 27.5 mM Mg(2+). The initial velocity for the C. vinosum enzyme was also found to be independent of the (saturating) concentration of Mg(2+) when total RuBP was varied in the assay. Thus the response to total RuBP by these two bacterial enzymes, which markedly differ in structure, was closely similar.

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Interaction of ribulose bisphosphate carboxylase/oxygenase with 2-carboxyhexitol 1,6-bisphosphates

Cited by 9 publications

References 25 publications

The inhibition of ribulose 1,5-bisphosphate carboxylase oxygenase by several 2-carboxyhexitol 1- and 6-phosphates

The inhibition of ribulose 1,5-bisphosphate carboxylase oxygenase by several 2-carboxyhexitol 1- and 6-phosphates

Active-site histidines in recombinant cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase examined by site-directed mutagenesis

The response to ribulose bisphosphate4? (RuBP4?) and RuBP-Mg2? in catalysis by structurally divergent RuBP carboxylase/oxygenases

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