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In molecular biology, the GHMP kinase family is a family of kinase enzymes . Members of this family include homoserine kinases EC 2.7.1.39 , galactokinases EC 2.7.1.6 , and mevalonate kinases EC 2.7.1.36 . These kinases make up the GHMP kinase superfamily of ATP -dependent enzymes .[1] enzymes are involved in the biosynthesis of isoprenes and amino acids as well as in carbohydrate metabolism . These enzymes contain, in their N-terminal section, a conserved Gly /Ser -rich region which is probably involved in the binding of ATP.[2] [3] C-terminal domain of homoserine kinase has a central alpha-beta plait fold and an insertion of four helices , which, together with the N-terminal fold, creates a novel nucleotide binding fold.[4]
References [ edit ]
^ Bork P, Sander C, Valencia A (January 1993). "Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases" . Protein Sci . 2 (1): 31–40. doi :10.1002/pro.5560020104 . PMC 2142297 PMID 8382990 . ^ Tsay YH, Robinson GW (February 1991). "Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase" . Mol. Cell. Biol . 11 (2): 620–31. doi :10.1128/MCB.11.2.620 . PMC 359713 PMID 1846667 . ^ Lee M, Leustek T (December 1999). "Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene". Arch. Biochem. Biophys . 372 (1): 135–42. doi :10.1006/abbi.1999.1481 . PMID 10562426 . ^ Zhou T, Daugherty M, Grishin NV, Osterman AL, Zhang H (December 2000). "Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily" . Structure . 8 (12): 1247–57. doi :10.1016/s0969-2126(00)00533-5 PMID 11188689 .
