Purification, Properties and Phosphorylation of Anaerobically Induced Enolase in Echinochloa phyllopogon and E. crus-pavonis |
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Authors: | Mujer Cesar V; Fox Theodore C; Williams Adrienne S; Andrews David L; Kennedy Robert A; Rumpho Mary E |
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Institution: | 1 Department of Horticultural Sciences, Texas A & M University College Station, TX 77843, U.S.A.
2 Department of Biology, Texas A & M University College Station, TX 77843, U.S.A. |
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Abstract: | Enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11
EC]
) activityis differentially induced by anoxia in the flood-tolerant speciesE. phyllopogon (Stev.) Koss and the flood-intolerant speciesE. crus-pavonis (H.B.K.) Schult. To examine the regulation ofenolase at the protein level, we purified the enzyme from bothspecies to near homogeneity and compared their physico-chemicaland catalytic properties. Enolase purified from E. phyllopogonexhibits optimal activity at pH 7.0, a Km of 80 µM for2-PGA, a Q10 of 1.97 and an Ea of 12.3 kcal mol-1. Similarly,enolase from E. crus-pavonis exhibits optimal activity at pH7.0, a Km of 50 µM for 2-PGA, a Q10 of 2.04 and an Eaof 12.9 kcal mol-1. The enzyme from both species is thermostable(100% active after 15 min, 50°C) and is a homodimer of 52.5kDa subunits as resolved by SDS-PAGE and immunoblotting. E.phyllopogon enolase was phosphorylated in vitro using either |
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