51-45-6Relevant articles and documents
The metabolism of histamine-beta-C.
BOUTHILLIER,GOLDNER
, p. 251 - 252 (1953)
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Chang,Snell
, p. 2005,2010 (1968)
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The intrinsic basicity of 4(5)-2′-aminoethylimidazole (histamine)
Hernández-Laguna,Abboud,Notario,Homan,Smeyers
, p. 1450 - 1454 (1993)
The gas-phase basicity (GB) of histamine (1) relative to ammonia (defined as the standard Gibbs energy change for reaction 1) has been measured by means of Fourier transform ion cyclotron resonance spectroscopy (FT-ICR): 1H+(g) + NH3(g) ? 1(g) + NH4+(g). The various tautomer/conformers of 1H+(g) were studied by means of ab initio SCF-LCAO-MO calculations at the 6-31G//6-31G level. The calculated proton affinity agrees well with that estimated from FT-ICR results. Ring protonation is slightly preferred over side-chain protonation. Chelation provides a major contribution to the stability of 1H+(g). Comparison of these results with aqueous solution data reveals dramatic differences due to solvation.
A single amino acid substitution converts a histidine decarboxylase to an imidazole acetaldehyde synthase
Takeshima, Daiki,Mori, Ayaka,Ito, Hideyuki,Komori, Hirofumi,Ueno, Hiroshi,Nitta, Yoko
, (2020)
Histidine decarboxylase (HDC; EC 4.1.1.22), an enzyme that catalyzes histamine synthesis with high substrate specificity, is a member of the group II pyridoxal 5′-phosphate (PLP) -dependent decarboxylase family. Tyrosine is a conserved residue among group II PLP-dependent decarboxylases. Human HDC has a Y334 located on a catalytically important loop at the active site. In this study, we demonstrated that a HDC Y334F mutant is capable of catalyzing the decarboxylation-dependent oxidative deamination of histidine to yield imidazole acetaldehyde. Replacement of the active-site Tyr with Phe in group II PLP-dependent decarboxylases, including mammalian aromatic amino acid decarboxylase, plant tyrosine/DOPA decarboxylase, and plant tryptophan decarboxylase, is expected to result in the same functional change, given that a Y-to-F substitution at the corresponding residue (number 260) in the HDC of Morganella morganii, another group II PLP-dependent decarboxylase, yielded the same effect. Thus, it was suggested that the loss of the OH moiety from the active-site Tyr residue of decarboxylase uniquely converts the enzyme to an aldehyde synthase.
Interaction pattern of histidine, carnosine and histamine with methylglyoxal and other carbonyl compounds
Ghassem Zadeh, Raheleh,Yaylayan, Varoujan
, (2021)
The ability of histidine to scavenge sugar-derived 1,2-dicarbonyl compounds was investigated using aqueous methanolic model systems containing histidine or histamine in the presence of glucose, methylglyoxal, or glyoxal. The samples were prepared either a
Organocatalytic Decarboxylation of Amino Acids as a Route to Bio-based Amines and Amides
Claes, Laurens,Janssen, Michiel,De Vos, Dirk E.
, p. 4297 - 4306 (2019/08/26)
Amino acids obtained by fermentation or recovered from protein waste hydrolysates represent an excellent renewable resource for the production of bio-based chemicals. In an attempt to recycle both carbon and nitrogen, we report here on a chemocatalytic, metal-free approach for decarboxylation of amino acids, thereby providing a direct access to primary amines. In the presence of a carbonyl compound the amino acid is temporarily trapped into a Schiff base, from which the elimination of CO2 may proceed more easily. After evaluating different types of aldehydes and ketones on their activity at low catalyst loadings (≤5 mol%), isophorone was identified as powerful organocatalyst under mild conditions. After optimisation many amino acids with a neutral side chain were converted in 28–99 % yield in 2-propanol at 150 °C. When the reaction is performed in DMF, the amine is susceptible to N-formylation. This consecutive reaction is catalysed by the acidity of the amino acid reactant itself. In this way, many amino acids were efficiently transformed to the corresponding formamides in a one-pot catalytic system.
