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- W1177291282 abstract "This chapter discusses the isolation and characterization of the uridylyl enzyme, galactose-1-phosphate uridylyltransferase. Galactose-1-P uridylyltransferase can be purified from Escherichia coli, human erythrocytes, and Saccharomyces cerevisiae. Of these, the enzyme from E. coli is the most thoroughly characterized with respect to molecular properties and mechanism of action. While characterizing the catalytic pathway followed by E. coli galactose-1-P uridylyltransferase, the steady state rates are found to be consistent only with the double displacement (Ping Pong Bi Bi) kinetic model. The intermediate uridylyl-enzyme implied by the model given in the chapter can be isolated in both catalytically active and fully denatured forms. The uridylyl group in this intermediate has been shown to be bonded to N-3 of a histidine residue, and uridylyl group transfer has been shown to proceed with net retention of stereochemical configuration at Pα of substrates, which is consistent with a double-displacement mechanism." @default.
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- W1177291282 date "1982-01-01" @default.
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- W1177291282 title "[2] Galactose-1-phosphate uridylyltransferase: Detection, isolation, and characterization of the uridylyl enzyme" @default.
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- W1177291282 doi "https://doi.org/10.1016/s0076-6879(82)87004-3" @default.
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