Purification and properties of a pyridoxal 5'-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15.

Tanase, Sumio; Guirard, Beverly M.; Snell, Esmond E.

doi:10.1016/s0021-9258(18)88842-1

Cited by 76 publications

(21 citation statements)

References 26 publications

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“…[5] Both L-Pen and D-Pen can interact with the vitamin cofactor pyridoxal-5′-phosphate (PLP) [6] but L-Pen is generally a better inhibitor of PLP-dependent enzymes because it is a better mimic of the L-amino acid substrate for these enzymes. Inhibition of several PLP-dependent enzymes by L-Pen or D-Pen or a racemic mixture have been previously studied; these include alanine aminotransferase, 7 aspartate aminotransferase, [8] glutamate decarboxylase, [9] histidine decarboxylase [10] and serine hydroxymethyl transferase. [11] Ingestion of D-Pen can also indirectly reduce activity of the PLP-dependent enzyme kynureninase by lowering pyridoxine levels.…”

Section: L-penicillamine Is a Mechanism-based Inhibitor Of Serine Palmitoyltransferase By Forming A Pyridoxal-5′-phosphate-thiazolidine Amentioning

confidence: 99%

l-Penicillamine is a mechanism-based inhibitor of serine palmitoyltransferase by forming a pyridoxal-5′-phosphate-thiazolidine adduct

et al. 2012

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Section: L-penicillamine Is a Mechanism-based Inhibitor Of Serine Palmitoyltransferase By Forming A Pyridoxal-5′-phosphate-thiazolidine Amentioning

confidence: 99%

l-Penicillamine is a mechanism-based inhibitor of serine palmitoyltransferase by forming a pyridoxal-5′-phosphate-thiazolidine adduct

et al. 2012

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“…Different from most amino acid decarboxylases, which could be determined by manometric, [10] radiometric [11] or optical methods, [12] the only reported approach to determine the MetDC enzymatic activity is the multistep colorimetric method with two further enzymatic reaction steps (Scheme 1a). [3,13] In this approach, the decarboxylated product of L-Met, 3-meth-ylthiopropylamine (3-MTP) is transformed to produce H 2 O 2 catalyzed by copper amine oxidase.…”

Section: Introductionmentioning

confidence: 99%

Monitoring Methionine Decarboxylase by a Supramolecular Tandem Assay

Zheng

Ren

Geng

et al. 2022

Chemistry An Asian Journal

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Methionine is an essential amino acid involved in many physiological and pathological processes. Methionine starvation caused by methionine decarboxylase (MetDC) degradation becomes a promising strategy for cancer treatment. Multistep colorimetric method, the present approach to monitor the MetDC activity, possesses drawbacks of the complicated process, low accuracy, and poor anti-interfer-ence due to indirect detection. Herein, we report a facile and easy-to-use supramolecular tandem assay (STA) with the cucurbit[7]uril and acridine orange reporter pair for the direct and real-time monitoring of MetDC activity. This strategy not only provides a feasible method for enzymatic activity detection but also establishes the capability of inhibitor screening.

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“…The existence of absorption bands at 416, 333, and 278 nm and the inactivation of the enzyme by NaCNBH3 indicate that the coenzyme is bound to the enzyme by an imine linkage to a lysine residue. The amino acid sequence near this lysine residue shows sequence homology with other PLP-dependent decarboxylases (Tañase et al, 1985). The protein sequence has been determined, and the gene for histidine decarboxylase has also been identified and sequenced (Vaaler et al, 1986; E. E. Snell, private communication).…”

mentioning

confidence: 97%

“…The pyruvoyl decarboxylases operate by a mechanism formally similar to that of the PLP decarboxylases: Both mechanisms involve an imine (Schiff base) linkage between substrate and cofactor, and the cofactor serves as an electron sink in the decarboxylation step. Both classes of enzymes show high structural specificity and stereospecificity (Rosenthaler et al, 1965;Tañase et al, 1985).…”

mentioning

confidence: 99%

Isotope effect studies of the pyridoxal 5'-phosphate dependent histidine decarboxylase from Morganella morganii

Abell¹,

O’Leary²

1988

Biochemistry

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The pyridoxal 5'-phosphate dependent histidine decarboxylase from Morganella morganii shows a nitrogen isotope effect k14/k15 = 0.9770 +/- 0.0021, a carbon isotope effect k12/k13 = 1.0308 +/- 0.0006, and a carbon isotope effect for L-[alpha-2H]histidine of 1.0333 +/- 0.0001 at pH 6.3, 37 degrees C. These results indicate that the overall decarboxylation rate is limited jointly by the rate of Schiff base interchange and by the rate of decarboxylation. Although the observed isotope effects are quite different from those for the analogous glutamate decarboxylase from Escherichia coli [Abell, L. M., & O'Leary, M. H. (1988) Biochemistry 27, 3325], the intrinsic isotope effects for the two enzymes are essentially the same. The difference in observed isotope effects occurs because of a roughly twofold difference in the partitioning of the pyridoxal 5'-phosphate-substrate Schiff base between decarboxylation and Schiff base interchange. The observed nitrogen isotope effect requires that the imine nitrogen in this Schiff base is protonated. Comparison of carbon isotope effects for deuteriated and undeuteriated substrates reveals that the deuterium isotope effect on the decarboxylation step is about 1.20; thus, in the transition state for the decarboxylation step, the carbon-carbon bond is about two-thirds broken.

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Purification and properties of a pyridoxal 5'-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15.

Cited by 76 publications

References 26 publications

l-Penicillamine is a mechanism-based inhibitor of serine palmitoyltransferase by forming a pyridoxal-5′-phosphate-thiazolidine adduct

l-Penicillamine is a mechanism-based inhibitor of serine palmitoyltransferase by forming a pyridoxal-5′-phosphate-thiazolidine adduct

Monitoring Methionine Decarboxylase by a Supramolecular Tandem Assay

Isotope effect studies of the pyridoxal 5'-phosphate dependent histidine decarboxylase from Morganella morganii

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