l-Dopa Upregulates the Expression and Activities of Methionine Adenosyl Transferase and Catechol-O-Methyltransferase

2001 ◽  
Vol 171 (1) ◽  
pp. 127-138 ◽  
Author(s):  
Wan-Qian Zhao ◽  
Lekan Latinwo ◽  
Xiao-Xiao Liu ◽  
Eun-Sook Lee ◽  
Nazarius Lamango ◽  
...  
Keyword(s):  
Methionine Adenosyl Transferase

scholarly journals Site-specific bioalkylation of rapamycin by the RapM 16-O-methyltransferase

2015 ◽  
Vol 6 (5) ◽  
pp. 2885-2892 ◽  
Author(s):  
Brian J. C. Law ◽  
Anna-Winona Struck ◽  
Matthew R. Bennett ◽  
Barrie Wilkinson ◽  
Jason Micklefield
Keyword(s):  
Site Specific ◽  
Coupled Reactions ◽  
Methionine Adenosyl Transferase

Characterisation of a rapamycin O-methyltransferase (RapM) and its utilisation in coupled reactions, with an improved variant of the human methionine adenosyl transferase (hMAT2A), results in new regioselectively alkylated rapamycin derivatives.

Methionine Adenosyltransferase, Cystathionine β-Synthase and Cystathionine γ-Iyase Activity of Rat Liver Subcellular Particles, Human Blood Cells and Mixed White Cells from Rat Bone Marrow

1975 ◽  
Vol 48 (6) ◽  
pp. 509-513
Author(s):  
Jennifer Allsop ◽  
R. W. E. Watts
Keyword(s):  
Bone Marrow ◽  
Rat Liver ◽  
Liver Homogenate ◽  
Methionine Adenosyltransferase ◽  
Cell Nuclei ◽  
Cytoplasmic Fraction ◽  
Cytosol Fraction ◽  
Human Blood Cells ◽  
Rat Liver Cells ◽  
Methionine Adenosyl Transferase

1. Methionine adenosyltransferase (ATP:l-methionine-S-adenosyl transferase, EC 2.5.1.6), cystathionine β-synthase [l-serine hydro-lyase (adding homocysteine), EC 4.2.1.22] and cystathionine γ-lyase [l-cystathionine cysteine-lyase (deaminating), EC 4.4.1.1] activities were found only in the cytosol fraction of rat liver cells. None was found in the mitochondrial or endoplasmic reticulum fractions as judged by the distribution of marker enzymes on a density gradient after centrifugation of the cytoplasmic fraction of a liver homogenate, or in a preparation of liver cell nuclei. 2. Polymorphs, lymphocytes (with admixed monocytes) and mixed bone marrow white cells contained no methionine adenosyl transferase, cystathionine β-synthase or cystathionine γ-lyase activities. 3. The possible bearing of these results on the problem of abnormal cystine storage in cystinosis is briefly discussed.

KINETIC STUDIES OF METHIONINE ADENOSYL TRANSFERASE IN AFFECTIVE DISORDERS AND SCHIZOPHRENIA

1984 ◽  
Vol 7 ◽  
pp. S56-S57
Author(s):  
L Tolbert ◽  
J. Monti ◽  
R. Alarcon ◽  
W. Walter-Ryan ◽  
J. Smythies
Keyword(s):  
Affective Disorders ◽  
Kinetic Studies ◽  
Methionine Adenosyl Transferase

Histological expression of methionine adenosyl transferase (MAT) 2A as a post-surgical prognostic surrogate in patients with hepatocellular carcinoma

2018 ◽  
Vol 117 (5) ◽  
pp. 892-901 ◽  
Author(s):  
Jihyun An ◽  
Seong Kyun Na ◽  
Ju Hyun Shim ◽  
Yang Soon Park ◽  
Mi Jung Jun ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Methionine Adenosyl Transferase

scholarly journals Distant Precursors of Benzylisoquinoline Alkaloids and their Enzymatic Formation

1987 ◽  
Vol 42 (4) ◽  
pp. 319-332 ◽  
Author(s):  
Martina Rueffer ◽  
Meinhart H. Zenk
Keyword(s):  
Isoquinoline Alkaloid ◽  
Conclusive Evidence ◽  
Alkaloid Biosynthesis ◽  
Enzymatic Formation ◽  
Tyrosine Metabolism ◽  
Protoberberine Alkaloid ◽  
Phenylpyruvate Decarboxylase ◽  
Isoquinoline Alkaloid Biosynthesis ◽  
Methionine Adenosyl Transferase

The incorporation rates of labelled tyrosine, DOPA. tyramine. and dopamine have been inves­tigated during the in vivo formation of the protoberberine alkaloid, jatrorrhizine, in callus cul­tures of Berberis canadensis. While tyrosine was equally well incorporated into both the iso­quinoline (54%) and benzyl (46%) portions of the alkaloid, DOPA was almost exclusively (91%) transformed into the isoquinoline moiety. However, tyramine (25%) and to a lesser extent, dopamine (15%) were incorporated into the aldehyde-derived, benzylic half of the isoquinoline molecule as well. In order to investigate further the precursory roles of these compounds, select enzymes involved in tyrosine metabolism in alkaloid-producing cell cultures have been studied. The occurrence of tyrosine decarboxylase, phenolase, transaminase, p-hydroxyphenylpyruvate decarboxylase, amineoxidase and methionine adenosyl transferase was demonstrated in suspen­sion cells of Berberis. These enzymes were partially purified and a preliminary characterization was performed. In the light of these and previous data, the differential metabolism of tyrosine and DOPA in the early steps of isoquinoline alkaloid biosynthesis is discussed. Conclusive evidence as to the biosynthetic origin of the phenylacetaldehydes which furnish the benzylic moiety of the alkaloids is precluded by the presence of both amineoxidase and phenylpyruvate decarboxylase activities in these cultures.

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