Pyridoxal Phosphate and Metal Ions as Cofactors for Histidine Decarboxylase

Guirard, Beverly M.; Snell, Esmond E.

doi:10.1021/ja01647a083

Cited by 38 publications

(16 citation statements)

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“…Loss of activity occurred which could not be fully restored by the addition of pyridoxal phosphate. The nature of the non-restorable loss in activity is not known; it was not restored by the addition of Fe3+ ions, reported to be essential (besides pyridoxal phosphate) for the activity of histidine decarboxylase from Lactobacillus (Guirard & Snell, 1954). To determine the role of pyridoxal Figure 7 shows the effect on histamine formation of varying the concentration of semicarbazide, with 50 % inhibition produced by 5 x 10-5M and 99-8 % by 1O-2M semicarbazide.…”

Section: Experiments In Vivomentioning

confidence: 99%

“…Loss of activity occurred which could not be fully restored by the addition of pyridoxal phosphate. The nature of the non-restorable loss in activity is not known; it was not restored by the addition of Fe3+ ions, reported to be essential (besides pyridoxal phosphate) for the activity of histidine decarboxylase from Lactobacillus (Guirard & Snell, 1954). To determine the role of pyridoxal phosphate alone the dialysed extracts were divided in two parts; pyridoxal phosphate was added to one part and the enzyme activity of the two was compared, thereby finding the difference in activity due solely to this cofactor.…”

Section: Experiments In Vitromentioning

confidence: 99%

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Observations on the inhibition of histamine formation

Kahlson¹,

Rosengren²,

Thunberg³

1963

The Journal of Physiology

129

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Section: Experiments In Vivomentioning

confidence: 99%

“…Loss of activity occurred which could not be fully restored by the addition of pyridoxal phosphate. The nature of the non-restorable loss in activity is not known; it was not restored by the addition of Fe3+ ions, reported to be essential (besides pyridoxal phosphate) for the activity of histidine decarboxylase from Lactobacillus (Guirard & Snell, 1954). To determine the role of pyridoxal phosphate alone the dialysed extracts were divided in two parts; pyridoxal phosphate was added to one part and the enzyme activity of the two was compared, thereby finding the difference in activity due solely to this cofactor.…”

Section: Experiments In Vitromentioning

confidence: 99%

Observations on the inhibition of histamine formation

Kahlson¹,

Rosengren²,

Thunberg³

1963

The Journal of Physiology

129

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“…Ornithine decarboxylase from Lactobacillus sp. strain 30a (32,33), a gift from Dr. Marvin L. Hackert, was prepared similarly. The concentration of the decarboxylase was determined with an extinction coefficient, E 280 nm 0.1% ϭ 1.34 (32).…”

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confidence: 99%

“…strain 30a (32,33), a gift from Dr. Marvin L. Hackert, was prepared similarly. The concentration of the decarboxylase was determined with an extinction coefficient, E 280 nm 0.1% ϭ 1.34 (32). A ϳ1.6 mg/ml solution in 100 mM phosphate, pH 6.3, 0.5 mM EDTA, was dialyzed overnight at 0°C against the same buffer made 1 mM in freshly prepared DTT just before use.…”

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confidence: 99%

Assembly of the Gigantic Hemoglobin of the Earthworm Lumbricus terrestris

Zhu

Ownby

Riggs

et al. 1996

Journal of Biological Chemistry

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The extracellular hemoglobin of the earthworm Lumbricus terrestris has four major kinds of O 2 -binding chains: a, b, and c (forming a disulfide-linked trimer), and chain d. Non-heme, non-globin structural chains, "linkers," are also present. Light-scattering techniques have been used to show that the ferrous CO-saturated abc trimer and chain d form an (abcd) 4 complex of 285 kDa at neutral pH. Formation of the full-sized 4-MDa molecule requires the addition of linker chains in the proportion of two linkers per (abcd) 4 and occurs much more rapidly in the presence of 10 mM calcium. This stoichiometry is supported not only by direct quantitative analysis of the intact hemoglobin but also by the fact that the addition of 50% of the proposed stoichiometric quantity of linkers results in the conversion of 50% of the (abcd) 4 to full-sized molecules. Isolated COsaturated abc trimers self-associate to (abc) 2 and higher aggregates up to an apparent limit of (abc) 10 ϳ550 kDa. The extracellular hemoglobins of annelids were first shown by Svedberg and Eriksson (1) to be gigantic molecules of at least 3 MDa in molecular mass. Although several subsequent studies gave molecular masses close to 4 MDa or higher for the Hb of Lumbricus terrestris and related species (2-4), recent studies by scanning transmission electron microscopy (5) have suggested masses of 3.5-3.6 MDa, and early light-scattering measurements suggested even lower values (6, 7). A possible reason for this great variation in reported molecular masses is oxidation which has been shown to cause extensive dissociation of many annelid Hbs (8 -10). Goss et al. (9) used light scattering to show that oxidation of L. terrestris Hb at neutral pH caused a large drop in molecular weight. Similarly, Ascoli et al. (10) found that oxidation of the similar Hb from Octolasium complanatum 1 caused hemichrome formation and dissociation outside of a narrow range near pH 7.The stoichiometry has also been uncertain. The Hb of L. terrestris has four major kinds of O 2 -binding globin chains: a, b, and c (forming the disulfide-linked abc trimer) and chain d, together with non-heme structural chains, "linkers," designated L. Kapp et al. (11) and Vinogradov et al. (12) have reported that linkers comprise 33-36% of the total mass, but this conclusion was based largely on the staining of SDS-gels with Coomassie Blue. This dye, however, binds to different proteins to quite different extents (13,14). Ownby et al. (15) redetermined the stoichiometry by reverse-phase high performance liquid chromatography (HPLC).2 The weight proportions of linkers were found to be approximately 16.4% by two independent procedures: the integrated absorption of the HPLC peaks and amino acid analysis of these peaks. These results led to the conclusion that the overall stoichiometry is (abcd) 2 L. This stoichiometry is further supported by the results of SDS-capillary gel electrophoresis monitored at 214 nm (see our companion study (16)).The goals of the present experiments are to redetermine the molecu...

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“…The general principles here outlined can be applied to the study of many other chemical reactions where both enzymatic and nonenzymatic processes are promoted by polyvalent metal ions. E. E. Snell and his collaborators 6 have shown that several of the enzlmatic reactions of pyridoxal can be carried out by substituting Cu + or Al +++ for the enzyme. In one instance, they were further able to show 7 that the enzymatic reaction requires a polyvalent ion (ferric ion) for activity.…”

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confidence: 99%

The Mechanisms of Some Metal‐ion‐promoted Reactions*

Westheimer

1955

Trans NY Acad Sci

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Pyridoxal Phosphate and Metal Ions as Cofactors for Histidine Decarboxylase

Cited by 38 publications

References 0 publications

Observations on the inhibition of histamine formation

Observations on the inhibition of histamine formation

Assembly of the Gigantic Hemoglobin of the Earthworm Lumbricus terrestris

The Mechanisms of Some Metal‐ion‐promoted Reactions*

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