Tian M, Mochizuki K, Loidl J (2022) Arrested crossover precursor structures form stable homologous bonds in a Tetrahymena meiotic mutant. PloS one 17(2):e0263691 PUBMED:35171923
Nabeel-Shah S, Garg J, Saettone A, Ashraf K, Lee H, Wahab S, Ahmed N, Fine J, Derynck J, Pu S, Ponce M, Marcon E, Zhang Z, Greenblatt JF, Pearlman RE, Lambert JP, Fillingham J (2021) Functional characterization of RebL1 highlights the evolutionary conservation of oncogenic activities of the RBBP4/7 orthologue in Tetrahymena thermophila. Nucleic acids research ( ): PUBMED:34086947
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Identifiers and Description
Gene Model Identifier
TTHERM_00486480
Standard Name
ENO1 (ENOlase 1)
Aliases
PreTt19579 | 59.m00217 | 3680.m00074
Description
ENO1 carboxy-terminal TIM barrel domain enolase; Enolase; portions of this gene may have been laterally transferred
ENO1 Enolase I, a phosphopyruv
ate hydratase that catalyzes t
he conversion of 2-phosphoglyc
erate to phosphoenolpyruvate d
uring glycolysis and the rever
se reaction during gluconeogen
esis; expression is repressed
in response to glucose
General Information
No Data fetched for General Information
Associated Literature
Ref:17785518: Kilburn CL, Pearson CG, Romijn EP, Meehl JB, Giddings TH, Culver BP, Yates JR, Winey M (2007) New Tetrahymena basal body protein components identify basal body domain structure. The Journal of cell biology 178(6):905-12
Ref:11526220: Keeling PJ and Palmer JD (2001) Lateral transfer at the gene and subgenic levels in the evolution of eukaryotic enolase. Proc Natl Acad Sci U S A 98(19):10745-50