Indispensable residue for uridine binding in the uridine-cytidine kinase family

Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on Tyr93, although the precise mec...

Descripción completa

Detalles Bibliográficos
Autores principales: Tomoike, Fumiaki, Nakagawa, Noriko, Fukui, Kenji, Yano, Takato, Kuramitsu, Seiki, Masui, Ryoji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5614712/
https://www.ncbi.nlm.nih.gov/pubmed/28955773
http://dx.doi.org/10.1016/j.bbrep.2017.07.002
_version_ 1783266449542873088
author Tomoike, Fumiaki
Nakagawa, Noriko
Fukui, Kenji
Yano, Takato
Kuramitsu, Seiki
Masui, Ryoji
author_facet Tomoike, Fumiaki
Nakagawa, Noriko
Fukui, Kenji
Yano, Takato
Kuramitsu, Seiki
Masui, Ryoji
author_sort Tomoike, Fumiaki
collection PubMed
description Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on Tyr93, although the precise mechanism remains unresolved. Exhaustive mutagenesis of Tyr93 in ttCK revealed that the uridine phosphorylation activity was restored only by replacement of Tyr93 with His or Gln. Replacement of His117 in human UCK2, corresponding to residue Tyr93 in ttCK, by Tyr resulted in a loss of uridine phosphorylation activity. These findings indicated that uridine phosphorylation activity commonly depends on a single residue in the UCK family.
format Online
Article
Text
id pubmed-5614712
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-56147122017-09-27 Indispensable residue for uridine binding in the uridine-cytidine kinase family Tomoike, Fumiaki Nakagawa, Noriko Fukui, Kenji Yano, Takato Kuramitsu, Seiki Masui, Ryoji Biochem Biophys Rep Research Article Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on Tyr93, although the precise mechanism remains unresolved. Exhaustive mutagenesis of Tyr93 in ttCK revealed that the uridine phosphorylation activity was restored only by replacement of Tyr93 with His or Gln. Replacement of His117 in human UCK2, corresponding to residue Tyr93 in ttCK, by Tyr resulted in a loss of uridine phosphorylation activity. These findings indicated that uridine phosphorylation activity commonly depends on a single residue in the UCK family. Elsevier 2017-07-08 /pmc/articles/PMC5614712/ /pubmed/28955773 http://dx.doi.org/10.1016/j.bbrep.2017.07.002 Text en © 2017 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Tomoike, Fumiaki
Nakagawa, Noriko
Fukui, Kenji
Yano, Takato
Kuramitsu, Seiki
Masui, Ryoji
Indispensable residue for uridine binding in the uridine-cytidine kinase family
title Indispensable residue for uridine binding in the uridine-cytidine kinase family
title_full Indispensable residue for uridine binding in the uridine-cytidine kinase family
title_fullStr Indispensable residue for uridine binding in the uridine-cytidine kinase family
title_full_unstemmed Indispensable residue for uridine binding in the uridine-cytidine kinase family
title_short Indispensable residue for uridine binding in the uridine-cytidine kinase family
title_sort indispensable residue for uridine binding in the uridine-cytidine kinase family
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5614712/
https://www.ncbi.nlm.nih.gov/pubmed/28955773
http://dx.doi.org/10.1016/j.bbrep.2017.07.002
work_keys_str_mv AT tomoikefumiaki indispensableresidueforuridinebindingintheuridinecytidinekinasefamily
AT nakagawanoriko indispensableresidueforuridinebindingintheuridinecytidinekinasefamily
AT fukuikenji indispensableresidueforuridinebindingintheuridinecytidinekinasefamily
AT yanotakato indispensableresidueforuridinebindingintheuridinecytidinekinasefamily
AT kuramitsuseiki indispensableresidueforuridinebindingintheuridinecytidinekinasefamily
AT masuiryoji indispensableresidueforuridinebindingintheuridinecytidinekinasefamily

Ejemplares similares