Results 231 to 240 of about 42,773 (253)

Characterization of ornithine decarboxylase with histidine decarboxylase activity in natural histidine decarboxylase gene deletion Enterobacter hormaechei RH3

Food Microbiology
Histamine is predominantly produced in sausages via the decarboxylation of histidine by bacteria. Furthermore, histamine-producing bacteria usually possess the enzyme histidine decarboxylase (hdc). Enterobacter hormaechei RH3 isolated from sausages exhibited significant levels of histamine production despite the absence of hdc.
Huijie, Pei, Yilun, Wang, Wei, He, Yue, Zhang, Lamei, Yang, Jinhai, Li, Yixuan, Ma, Xinjie, Hu, Shuhong, Li, Jianlong, Li, Kaidi, Hu, Aiping, Liu, Xiaolin, Ao, Hui, Teng, Ran, Li, Qin, Li, Likou, Zou, Shuliang, Liu, Yong, Yang   +18 more
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[227] Histidine decarboxylase (mammalian)

1971
Publisher Summary This chapter discusses the methods of preparation of Histidine Decarboxylase (Mammalian). Two kinetically different histamine-forming enzymes or groups of enzymes have been demonstrated in mammalian tissues. One is possibly identical with the nonspecific aromatic L -amino acid decarboxylase also referred to as L -DOPA ...
Dorothea Aures, Rolf Håkanson
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Reaction of Lactobacillus histidine decarboxylase with L-histidine methyl ester

Biochemistry, 1987
L-Histidine methyl ester inactivates histidine decarboxylase in a time-dependent manner. The possibility was considered that an irreversible reaction between enzyme and inhibitor occurs [Recsei, P. A., & Snell, E. E. (1970) Biochemistry 9, 1492-1497].
T A, Alston, R H, Abeles
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Effect of metabolite antagonists on histidine decarboxylase*

Journal of the American Pharmaceutical Association (Scientific ed.), 1949
The results of a study of histidine decarboxylase metabolite antagonists are reported. The compounds used in the study included a series of vitamin antagonists, compounds containing phenolic hydroxyl groups and compounds structurally related to histidine.
J.M. Beiler, Robert Brendel, Miriam Graff, Gustav J. Martin   +3 more
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Histidine decarboxylase in the fetal rat

Biochemical Pharmacology, 1963
Abstract The properties of a purified preparation of histidine decarboxylase from fetal rat tissues have been studied. From kinetic data there is reason to believe that the enzyme requires the anionic form of the substrate and that the active form of the enzyme occurs more abundantly at acid pH. Pyridoxal-5-phosphate is required as a coenzyme.
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Histidine decarboxylase: Isolation and molecular characteristics

Neurochemical Research, 1984
High levels of histidine decarboxylase activity were measured in rat basophilic leukemia cells grown in ascitic form in 4 week old WKY/N rats. The potent inhibition of this enzyme by brocresine and alpha-methylhistidine but not by alpha-methyl DOPA identified it as a specific histidine decarboxylase.
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Mammalian Histidine Decarboxylase and DOPA Decarboxylase

Annals of the New York Academy of Sciences, 1990
H, Wada, M, Taketoshi, I, Imamura, T, Tanaka, Y, Horio, Y, Taguchi, H, Fukui   +6 more
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Kinetic properties of mammalian histidine decarboxylase

European Journal of Pharmacology, 1967
Abstract Semi-purified preparations of histidine decarboxylase from hamster placenta and from fetal rat tissues have been studied. The properties of the histamine-forming enzyme from hamster placenta are very similar to those of fetal rat histidine decarboxylase.
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Inhibition of histidine decarboxylases

Biochimica et Biophysica Acta, 1961
B, ROBINSON, D M, SHEPHERD
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Formation of Histamine: Histidine Decarboxylase

1991
Histidine decarboxylase (HDC, L -histidine carboxylyase, EC 4.1.1.22) catalyses the decarboxylation of L -histidine to histamine. It is the only enzyme that forms histamine (Schayer 1966, 1978). There have been a great number of papers on histamine (including more than ten monographs), but it is only recently that studies on HDC have been carried out ...
T. Watanabe, Y. Taguchi, K. Maeyama, H. Wada   +3 more
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