The Significance of Amino Acid Residue Asp446 for Enzymatic Stability of Rat UDP-Glucuronosyltransferase UGT1A6

1999 ◽  
Vol 363 (1) ◽  
pp. 116-120 ◽  
Author(s):  
Hidetomo Iwano ◽  
Hiroshi Yokota ◽  
Satoru Ohgiya ◽  
Akira Yuasa
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Enzymatic Stability ◽  
Udp Glucuronosyltransferase

scholarly journals A critical amino acid residue, Asp446, in UDP-glucuronosyltransferase

1997 ◽  
Vol 325 (3) ◽  
pp. 587-591 ◽  
Author(s):  
Hidetomo IWANO ◽  
Hiroshi YOKOTA ◽  
Satoru OHGIYA ◽  
Naomi YOTUMOTO ◽  
Akira YUASA
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Amino Acid Substitution ◽  
Critical Role ◽  
Enzymic Activity ◽  
Male Rat ◽  
Transferase Activity ◽  
Rt Pcr ◽  
Taq Polymerase ◽  
Udp Glucuronosyltransferase

An amino acid residue, Asp446, was found to be essential for the enzymic activity of UDP-glucuronosyltransferase (UGT). We obtained a rat phenol UGT (UGT1*06) cDNA (named Ysh) from male rat liver by reverse-transcription (RT)-PCR using pfu polymerase. A mutant Ysh having two different bases, A1337G and G1384A (named Ysh A1337GC1384A), that result in two amino acid substitutions, D446G and V462M, was obtained by RT-PCR using Taq polymerase. Ysh was expressed functionally in microsomes of Saccharomyces cerevisiae strain AH22. However, the expressed protein from Ysh A1337GG1384A had no transferase activity. Two other mutant cDNAs with Ysh A1337G having one changed base, A1337G, resulting in one amino acid substitution, D446G, and Ysh G1384A having a changed base, G1384A, resulting in an amino acid substitution, V462M, were constructed and expressed in the yeast. The expressed protein from Ysh G1384A (named Ysh V462M) exhibited enzymic activity, but the one from Ysh A1337G (named Ysh D446G) did not show any activity at all. Asp446 was conserved in all UGTs and UDP-galactose:ceramide galactosyltransferases reported, suggesting that Asp446 plays a critical role in each enzyme.

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

scholarly journals Amino Acid Residue at the 165th Position Tunes Eyfp Chromophore Maturation. A Structure-Based Design

2021 ◽  
Author(s):  
Nadya V. Pletneva ◽  
Eugene G. Maksimov ◽  
Elena A. Protasova ◽  
Anastasia V. Mamontova ◽  
Tatiana R. Simonyan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue

scholarly journals Effect of roasting temperature on lipid and protein oxidation and amino acid residue side chain modification of beef patties

RSC Advances ◽  
2021 ◽  
Vol 11 (35) ◽  
pp. 21629-21641
Author(s):  
Chao Xia ◽  
Pingping Wen ◽  
Yaming Yuan ◽  
Xiaofan Yu ◽  
Yijing Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Protein Oxidation ◽  
Relative Number ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Beef Patties ◽  
Lipid And Protein Oxidation ◽  
Roasting Temperature

The relative number of peptides modified by the amino acid residues of actin from raw beef patties and those cooked at different roasting temperatures.

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