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Propylamine transferase

One of two novel transferases reported recently is the tetrahydromethanopterin methyltransferase involved in methanogenesis in Methanobacterium thermoautotrophicum [180]. No thermostability data on the oxygen sensitive enzyme were presented. The second enzyme is the propylamine transferase studied in the archaebacterium Sulfolobus solfataricus [181]. This enzyme (optimum pH 7.5) appears to be solely responsible for transfer of the aminopropyl residue from S-adenosyl (5 )-3-methylthiopropylamine to various acceptors. [Pg.76]

Bolhnger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT (1995) Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J Biol Chem 270 14031-14041 Bowman WH, Tabor CW, Tabor H (1973) Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli. J Biol Chem 248 2480-2486 Chattopadhyay MK, Tabor CW, Tabor H (2009) Polyamines are not required for aerobic growth of Escherichia coli preparation of a strain with deletions in all of the genes for polyamine biosynthesis. JBacteriol 191 5549-5552... [Pg.57]


See other pages where Propylamine transferase is mentioned: [Pg.211]    [Pg.435]    [Pg.211]    [Pg.435]    [Pg.599]    [Pg.599]    [Pg.37]   


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Propylamin

Propylamine

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