| First Author | Griffin LD | Year | 1991 |
| Journal | Genomics | Volume | 11 |
| Issue | 4 | Pages | 1014-24 |
| PubMed ID | 1783373 | Mgi Jnum | J:12690 |
| Mgi Id | MGI:60005 | Doi | 10.1016/0888-7543(91)90027-c |
| Citation | Griffin LD, et al. (1991) Mammalian hexokinase 1: evolutionary conservation and structure to function analysis. Genomics 11(4):1014-24 |
| abstractText | We have amplified and sequenced the complete coding region of bovine hexokinase isoenzyme 1 (HK1) from brain RNA with PCR primers selected for sequence conservation. The sequence information was analyzed to evaluate the evolutionary and structure-function relationships among the mammalian and yeast HK isoenzymes. Structure to function analysis identified an unduplicated, invariant N-terminal domain involved in HK1 outer mitochondrial membrane targeting, as well as putative carbohydrate and nucleotide-binding sites in the regulatory and catalytic halves of HK1 essential to enzyme function. The ATP-binding site in the catalytic half of the HK1 protein resembles nucleotide-binding regions from protein kinases, with the single amino acid replacement (lysine to glutamate) in the ATP-binding site of the amino half explaining the loss of HK1 catalytic function in the regulatory domain. Sequence comparisons suggest that the 50-kDa mammalian and yeast glucokinases arose separately in evolution. In addition to providing valuable phylogenetic and structure-function insights, this work provides an efficient strategy for rapid cloning and sequencing of the coding regions for other HKs and related proteins. |
