Formyltetrahydrofolate synthetase: Mechanism of cation activation

Himes, Richard H.; Wilder, Teresa

doi:10.1016/s0926-6593(65)80200-4

Cited by 30 publications

(14 citation statements)

References 14 publications

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“…Studies showed that chemically synthesized XPO can participate in both the forward and reverse reactions by formylating THF or phosphorylating ADP, respectively 18, 19. The finding that 18 O is transferred from formate to inorganic phosphate during the forward reaction15 further supports the involvement of this intermediate.…”

Section: Introductionsupporting

confidence: 54%

“…Numerous experiments have been performed to determine the mechanism by which FTHFS operates. It has been suggested that FTHFS employs a random sequential mechanism (random ter ter mechanism)12–14 on the basis of steady‐state kinetic data12 and isotope exchange experiments 8, 15. However, a more recent, careful kinetic study of FTHFS reports inhibition of the reaction by higher concentrations of THF 9.…”

Section: Introductionmentioning

confidence: 99%

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Cover Picture: Tailoring Copper Oxide Semiconductor Nanorod Arrays for Photoelectrochemical Reduction of Carbon Dioxide to Methanol (ChemPhysChem 10/2013)

et al. 2013

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O hybrid nanorod arrays are prepared on a Cu substrate by K. Rajeshwar, N. R. de Tacconi et al. (p. 2251). The procedure involves the initial thermal growth of CuO nanorods followed by controlled electrodeposition of p-type Cu 2 O crystallites on their walls. Photoelectrosynthesis of methanol from CO 2 is conducted under simulated solar irradiation at Faradaic efficiencies up to 95%. The hybrid nanoarchitectures, ensuring a double pathway for photoelectron injection to CO 2 , along with the high surface area are key to the excellent performance of these films.

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Section: Introductionsupporting

confidence: 54%

Section: Introductionmentioning

confidence: 99%

Cover Picture: Tailoring Copper Oxide Semiconductor Nanorod Arrays for Photoelectrochemical Reduction of Carbon Dioxide to Methanol (ChemPhysChem 10/2013)

et al. 2013

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“…The reaction mixtures were then allowed to stand at room temperature for 10 min. The absorbance of methenyl-H 4 F was determined at 350 nm (ε ϭ 24.9 mM Ϫ1 cm Ϫ1 [16]). Protein purification.…”

Section: Methodsmentioning

confidence: 99%

Purification of the Formate-Tetrahydrofolate Ligasefrom Methylobacterium extorquens AM1 and Demonstrationof Its Requirement for MethylotrophicGrowth

Marx¹,

Laukel

Vorholt

et al. 2003

J Bacteriol

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The serine cycle methylotroph Methylobacterium extorquens AM1 contains two pterin-dependent pathways for C 1 transfers, the tetrahydrofolate (H 4 F) pathway and the tetrahydromethanopterin (H 4 MPT) pathway, and both are required for growth on C 1 compounds. With the exception of formate-tetrahydrofolate ligase (FtfL, alternatively termed formyl-H 4 F synthetase), all of the genes encoding the enzymes comprising these two pathways have been identified, and the corresponding gene products have been purified and characterized. We present here the purification and characterization of FtfL from M. extorquens AM1 and the confirmation that this enzyme is encoded by an ftfL homolog identified previously through transposon mutagenesis. Phenotypic analyses of the ftfL mutant strain demonstrated that FtfL activity is required for growth on C 1 compounds. Unlike mutants defective for the H 4 MPT pathway, the ftfL mutant strain does not exhibit phenotypes indicative of defective formaldehyde oxidation. Furthermore, the ftfL mutant strain remained competent for wild-type conversion of [ 14 C]methanol to [ 14 C]CO 2 . Collectively, these data confirm our previous presumptions that the H 4 F pathway is not the key formaldehyde oxidation pathway in M. extorquens AM1. Rather, our data suggest an alternative model for the role of the H 4 F pathway in this organism in which it functions to convert formate to methylene H 4 F for assimilatory metabolism.

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“…Although SYN is encoded by a single gene in Arabidopsis (Hanson et al, 2000), in pea, its activity has been demonstrated in cytosol, mitochondria, and chloroplasts . This ATPdependent enzyme condenses formate and THF to 10-formyl THF, but it is potentially reversible with an equilibrium constant K eq being between 20 and 61 (Himes and Rabinowitz, 1962). Under photorespiratory conditions (ambient CO 2 levels) the concentrations of THF and 10-formyl THF in plant mitochondria likely favor the formation of formate and THF.…”

Section: Functions Of At4g17360 and At5g47435 Proteins In Photorespirmentioning

confidence: 99%

Arabidopsis 10-Formyl Tetrahydrofolate Deformylases Are Essential for Photorespiration

et al. 2008

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In prokaryotes, PurU (10-formyl tetrahydrofolate [THF] deformylase) metabolizes 10-formyl THF to formate and THF for purine and Gly biosyntheses. The Arabidopsis thaliana genome contains two putative purU genes, At4g17360 and At5g47435. Knocking out these genes simultaneously results in plants that are smaller and paler than the wild type. These double knockout (dKO) mutant plants show a 70-fold increase in Gly levels and accumulate elevated levels of 5-and 10-formyl THF. Embryo development in dKO mutants arrests between heart and early bent cotyledon stages. Mature seeds are shriveled, accumulate low amounts of lipids, and fail to germinate. However, the dKO mutant is only conditionally lethal and is rescued by growth under nonphotorespiratory conditions. In addition, culturing dKO siliques in the presence of sucrose restores normal embryo development and seed viability, suggesting that the seed and embryo development phenotypes are a result of a maternal effect. Our findings are consistent with the involvement of At4g17360 and At5g47435 proteins in photorespiration, which is to prevent excessive accumulation of 5-formyl THF, a potent inhibitor of the Gly decarboxylase/Ser hydroxymethyltransferase complex. Supporting this role, deletion of the At2g38660 gene that encodes the bifunctional 5,10-methylene THF dehydrogenase/5,10-methenyl THF cyclohydrolase that acts upstream of 5-formyl THF formation restored the wild-type phenotype in dKO plants.

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Formyltetrahydrofolate synthetase: Mechanism of cation activation

Cited by 30 publications

References 14 publications

Cover Picture: Tailoring Copper Oxide Semiconductor Nanorod Arrays for Photoelectrochemical Reduction of Carbon Dioxide to Methanol (ChemPhysChem 10/2013)

Cover Picture: Tailoring Copper Oxide Semiconductor Nanorod Arrays for Photoelectrochemical Reduction of Carbon Dioxide to Methanol (ChemPhysChem 10/2013)

Purification of the Formate-Tetrahydrofolate Ligasefrom Methylobacterium extorquens AM1 and Demonstrationof Its Requirement for MethylotrophicGrowth

Arabidopsis 10-Formyl Tetrahydrofolate Deformylases Are Essential for Photorespiration

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