Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities

MacKenzie, Robert E.; Baugh, Charles M.

doi:10.1016/0005-2744(80)90054-6

Cited by 78 publications

(49 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mackenzie and Baugh (9) showed that an enzyme for histidine oxidation preferred H4PteGlu5 as substrate and is regulated with the polyglutamate chain length by a metabolic channeling system. Fell and Steele (3) showed that the histidine catabolism was depressed and the urinary excretion of formiminoglutamate was increased in rats fed 1000 casein diets with 0.6% methionine and 1% histidine.…”

Section: Discussionmentioning

confidence: 99%

“…H4PteGlu5 was exhausted likely to its basal level, and H4PteGlu concentration was 2-fold higher than control, although CH3-H4PteGlu5 was markedly accumu lated in the 3.5%, histidine-supplemented rats. A bifunctional enzyme for histidine oxidation system has preferred H4PteGlu5 as substrate (9). This evidence suggests that the activity for catabolizing the large influx of histidine might be elevated and its activity might overcome the regenerating activity for folate cofactors such as methionine synthase.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Effect of a histidine-excess diet on a tetrahydrofolylpolyglutamate pattern in rat liver.

Kohashi

Takahashi

Iwai

1990

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

View full text Add to dashboard Cite

SummaryThe effect of a histidine-excess diet on the hepatic folylpol yglutamate pattern in rat was studied. Rats were fed ad libitum 9.7 casein basal diets with 0.6% methionine (controls) or the basal diets with 3.5% histidine. The average daily weight gain and the food intake in histidine-supplemented rats (His-rats) did not significantly differ from controls. The liver weight in His-rats, however, was 50% higher than controls.Hepatic methyltetrahydropteroylpentaglutamate (CH3 H4PteGlu5), and tetrahydropteroylmonoglutamate concentrations in His rats was 5.7 and 2-fold higher than controls, respectively. The tetrahyd ropteroylpentaglutamate (H4PteGlu5) concentration in the His-rats was 74% lower than controls. Considering the homeostasis of folate cofactors in tissues, these results suggest that the hepatic regeneration systems for H4PteGlu5 in His-rats might be repressed and an apparent methylfolate trap might be attained rather on a pteroylpentaglutamate level than a monoglutamate level, and that the activity for catabolizing the excess histidine might exceed the regenerating activity for folate cofactors. Key Words excess-histidine, liver, tetrahydrofolylpolyglutamate, methyl tetrahydrofolylpolyglutamate, methyl trapThe growth retardation, liver enlargement, and stimulation of cholestero genesis has been observed in rats fed excess-histidine diets (1). There are a few reports on the effect of an excess-histidine diet on folate metabolism.An in vivo catabolism of histidine through the one-carbon pool is mediated by folate-dependent enzymes (2) and modulated by methionine metabolism (3-5). It is now accepted that folylpolyglutamates rather than the monoglutamate are the acceptors and donors of one-carbon units in amino acid and nucleotide metabolism

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Effect of a histidine-excess diet on a tetrahydrofolylpolyglutamate pattern in rat liver.

Kohashi

Takahashi

Iwai

1990

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

View full text Add to dashboard Cite

show abstract

“…It is possible that p60 can oligomerize into a protein complex sufficiently large to cosediment with microtubules. FTCD is known to assemble into an octameric protein complex of identical subunits arranged as a circular tetramer of dimers (36,37,45), channelling polyglutamylated folate between its two types of catalytic sites (47,48). Protein complexes within that range of molecular mass (ϳ500 kDa), including coatomer, may be found under certain conditions in microtubule pellets.…”

Section: Discussionmentioning

confidence: 99%

A Formiminotransferase Cyclodeaminase Isoform Is Localized to the Golgi Complex and Can Mediate Interaction of Trans-Golgi Network-derived Vesicles with Microtubules

Hennig

Scales

Moreau

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

264, 16083-16092), is identical to FTCD. Both proteins co-purify with microtubules and co-localize with membranes of the Golgi complex. The capacity of FTCD to bind both to microtubules and Golgi-derived membranes may suggest that this protein, or one of its isoforms, might have in addition to its enzymatic activity, a second physiological function in mediating interaction of Golgi-derived membranes with microtubules.

show abstract

“…In such case, the increased affinity of the enzyme for polyglutamate substrates will appear as an increase in Vmax rather than as a decrease in Km for the folate substrate. Finally, polyglutamate substrates may be channeled from one active site to another in multifunctional proteins, or in macromolecular complexes of enzymes while the more weakly bound monoglutamate substrates dissociate and then rebind (23).…”

Section: Effects Of Substrate Polyglutamylation On Catalysismentioning

confidence: 99%

Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes

Matthews

Ghose

Green

et al. 1987

Advances in Enzyme Regulation

View full text Add to dashboard Cite

Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities

Cited by 78 publications

References 22 publications

Effect of a histidine-excess diet on a tetrahydrofolylpolyglutamate pattern in rat liver.

Effect of a histidine-excess diet on a tetrahydrofolylpolyglutamate pattern in rat liver.

A Formiminotransferase Cyclodeaminase Isoform Is Localized to the Golgi Complex and Can Mediate Interaction of Trans-Golgi Network-derived Vesicles with Microtubules

Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes

Contact Info

Product

Resources

About