Phosphomevalonic kinase

TSAY, Y.H., ROBINSON, G.W., Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase, Mol. Cell. Biol., 1991,11,620-631. 

PHOSPHOFRUCTOKINASE 3-PHOSPHOGLYCERATE KINASE 5-PHOSPHOMEVALONATE KINASE PHOSPHORYLASE KINASE POLYNUCLEOTIDE 5 -HYDROXYL KINASE... 

PHOSPHOLIPASE A2 PHOSPHOLIPASE B PHOSPHOLIPASE C PHOSPHOLIPASE D PHOSPHOLIPID FLIP-FLOP PHOSPHOMANNOMUTASE (R)-5-Phosphomevalonate, as substrate, 5-PHOSPHOMEVALONATE KINASE 5-PHOSPHOMEVALONATE KINASE... 

Eyzaguirre, J. Bazaes, S. Phosphomevalonate kinase from pig liver. Methods EnzymoL, 110, 78-85 (1985)... 

Bazaes, S. Beytia, E. Jabalquinto, A.M. Solis de Ovando, E Gomez, I. Pig liver phosphomevalonate kinase. 2. Participation of cysteinyl and lysyl groups in catalysis. Biochemistry, 19, 2305-2310 (1980)... 

Schulte, A.E. Van der Heijden, R. Verpoorte, R. Purification and characterization of phosphomevalonate kinase from Catharanthus roseus. Phytochemistry, 52, 975-983 (1999)... 

Romanowski, M.J. Bonanno, J.B. Burley, S.K. Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily. Proteins Struct. Fund. Genet., 47, 568-571 (2002)... 

Mevalonic acid, the product of HMGR, is converted to IPP by the sequential action of three enzymes mevalonate kinase, phosphomevalonate kinase and diphosphomevalonate decarboxylase (Fig. 5.3). These three catalysts have not previously been considered to be important control points in plant terpenoid biosynthesis, and little new information has appeared to alter this view. The... 

Full details have appeared of the rubber enzyme phosphomevalonate kinase (EC 2.7.4.2) and 5-pyrophosphomevalonate decarboxylase (EC 4.1.1.33). 

Phosphomevalonate kinase (PMK, EC 2.7.4.2) is the enzyme involved in the second step of the terpenoid biosynthesis and catalyzes the reversible conversion of mevalonate 5-phosphate and ATP to mevalonate 5-diphosphate and ADP, a key step in that synthesis. Fig. (6), [289-290]. Kinetic characterisation of PMK has been carried out using enzymes from mainly animal sources including human, S. cerevisiae and some plants. In addition, PMK has only been partially purified and characterized. It seems that this enzyme is quite a unique enzyme, but its characteristics reveal some remarkable differences among diverse sources. Thus, pig liver and human liver PMKs show molecular weights between 21 and 22 kDa [291-292], whereas the enzyme isolate from S. cerevisiae has a molecular weight of 47 kDa [293]. 

In a series of cytoplasmic reactions, mevalonate is subsequently converted to famesylpyrophosphate. Mevalonate kinase catalyzes the synthesis of phospho-mevalonate. A second phosphorylation reaction catalyzed by phosphomevalonate kinase produces 5-pyrophosphomevalonate. 

Mevalonate kinase Phosphomevalonate kinase Mevalonate PP decarboxylase GPP synthase IPP isomerase FPP synthase Squalene synthase... 

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