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Literature summary for 2.4.1.17 extracted from

  • Fujiwara, R.; Nakajima, M.; Yamamoto, T.; Nagao, H.; Yokoi, T.
    In silico and in vitro approaches to elucidate the thermal stability of human UDP-glucuronosyltransferase (UGT) 1A9 (2009), Drug Metab. Pharmacokinet., 24, 235-244.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
construction of three-dimensional structure by homology modeling using a crystal structure of TDP-epi-vancosaminyltransferase as template. Amino acid residues Arg42, Lys91, Ala92, Tyr106, Gly111, Tyr113, Asp115, Asn152, Leu173, Leu219, His221, Arg222, and Glu241 are unique to UGT1A9 as compared with UGT1A7, UGT1A8 and UGT1A10. Molecular dynamics simulation of the structures revealed that Arg42, Leu173, Leu219, His221 and Arg222 as well as residues Lys91, Ala92, Tyr106, Gly111, Tyr113, Asp115, and Glu241 are responsible for the thermal stability Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O60656 isoform UGT1A9
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Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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isoform UGT1A9 is rather stable against heat treatment. Molecular dynamics simulation of the structures revealed that Arg42, Leu173, Leu219, His221 and Arg222 as well as residues Lys91, Ala92, Tyr106, Gly111, Tyr113, Asp115, and Glu241 are responsible for the thermal stability Homo sapiens