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putative PEP-binding protein
This entry represents a TIM barrel domain found at the C terminus of a number of PEP (phosphoenolpyruvate)-utilising proteins. In PPDK (Pyruvate phosphate dikinase) this C-terminal domain has been shown to be a PEP-binding domain [1]. [1]. 18052212. Swiveling domain mechanism in pyruvate phosphate dikinase.. Lim K, Read RJ, Chen CC, Tempczyk A, Wei M, Ye D, Wu C,. Dunaway-Mariano D, Herzberg O;. Biochemistry. 2007;46:14845-14853. (from Pfam)
PEP-utilizing enzyme
This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it. [1]. 8610096. Swiveling-domain mechanism for enzymatic phosphotransfer between. remote reaction sites.. Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ,. Dunaway-Mariano D;. Proc Natl Acad Sci U S A 1996;93:2652-2657. (from Pfam)
PEP/pyruvate-binding domain-containing protein
This enzyme catalyses the reversible conversion of ATP to AMP, pyrophosphate and phosphoenolpyruvate (PEP). The N-terminal domain has been shown to be the AMP/ATP-binding domain [1]. [1]. 18052212. Swiveling domain mechanism in pyruvate phosphate dikinase.. Lim K, Read RJ, Chen CC, Tempczyk A, Wei M, Ye D, Wu C,. Dunaway-Mariano D, Herzberg O;. Biochemistry. 2007;46:14845-14853. (from Pfam)
phosphoenolpyruvate synthase
phosphoenolpyruvate synthase catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate
pyruvate, water dikinase
Also called pyruvate,water dikinase and PEP synthase. The member from Methanococcus jannaschii contains a large intein. This enzyme generates phosphoenolpyruvate (PEP) from pyruvate, hydrolyzing ATP to AMP and releasing inorganic phosphate in the process. The enzyme shows extensive homology to other enzymes that use PEP as substrate or product. This enzyme may provide PEP for gluconeogenesis, for PTS-type carbohydrate transport systems, or for other processes.
Catalyzes the formation of phosphoenolpyruvate from pyruvate
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