Glycerol kinase

Details

Name
Glycerol kinase
Synonyms
  • 2.7.1.30
  • ATP:glycerol 3-phosphotransferase
  • GK
  • Glycerokinase
Gene Name
glpK
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011141|Glycerol kinase
MTEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSST
LVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDG
LEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVH
VTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPI
SGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVN
YALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPY
ARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLM
QFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTER
NYRYAGWKKAVKRAMAWEEHDE
Number of residues
502
Molecular Weight
56230.375
Theoretical pI
5.18
GO Classification
Functions
ATP binding / glycerol kinase activity / metal ion binding / zinc ion binding
Processes
cellular response to DNA damage stimulus / glycerol catabolic process / glycerol metabolic process / glycerol-3-phosphate metabolic process / phosphorylation
Components
cytoplasm / cytosol
General Function
Zinc ion binding
Specific Function
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011142|Glycerol kinase (glpK)
ATGACTGAAAAAAAATATATCGTTGCGCTCGACCAGGGCACCACCAGCTCCCGCGCGGTC
GTAATGGATCACGATGCCAATATCATTAGCGTGTCGCAGCGCGAATTTGAGCAAATCTAC
CCAAAACCAGGTTGGGTAGAACACGACCCAATGGAAATCTGGGCCACCCAAAGCTCCACG
CTGGTAGAAGTGCTGGCGAAAGCCGATATCAGTTCCGATCAAATTGCAGCTATCGGTATT
ACGAACCAGCGTGAAACCACTATTGTCTGGGAAAAAGAAACCGGCAAGCCTATCTATAAC
GCCATTGTCTGGCAGTGCCGTCGTACCGCAGAAATCTGCGAGCATTTAAAACGTGACGGT
TTAGAAGATTATATCCGCAGCAATACCGGTCTGGTGATTGACCCGTACTTTTCTGGCACC
AAAGTGAAGTGGATCCTCGACCATGTGGAAGGCTCTCGCGAGCGTGCACGTCGTGGTGAA
TTGCTGTTTGGTACGGTTGATACGTGGCTTATCTGGAAAATGACTCAGGGCCGTGTCCAT
GTGACCGATTACACCAACGCCTCTCGTACCATGTTGTTCAACATCCATACCCTGGACTGG
GACGACAAAATGCTGGAAGTGCTGGATATTCCGCGCGAGATGCTGCCAGAAGTGCGTCGT
TCTTCCGAAGTATACGGTCAGACTAACATTGGCGGCAAAGGCGGCACGCGTATTCCAATC
TCCGGGATCGCCGGTGACCAGCAGGCCGCGCTGTTTGGTCAGTTGTGCGTGAAAGAAGGG
ATGGCGAAGAACACCTATGGCACTGGCTGCTTTATGCTGATGAACACTGGCGAGAAAGCG
GTGAAATCAGAAAACGGCCTGCTGACCACCATCGCCTGCGGCCCGACTGGCGAAGTGAAC
TATGCGTTGGAAGGTGCGGTGTTTATGGCAGGCGCATCCATTCAGTGGCTGCGCGATGAA
ATGAAGTTGATTAACGACGCCTACGATTCCGAATATTTCGCCACCAAAGTGCAAAACACC
AATGGTGTGTATGTGGTTCCGGCATTTACCGGGCTGGGTGCGCCGTACTGGGACCCGTAT
GCGCGCGGGGCGATTTTCGGTCTGACTCGTGGGGTGAACGCTAACCACATTATACGCGCG
ACGCTGGAGTCTATTGCTTATCAGACGCGTGACGTGCTGGAAGCGATGCAGGCCGACTCT
GGTATCCGTCTGCACGCCCTGCGCGTGGATGGTGGCGCAGTAGCAAACAATTTCCTGATG
CAGTTCCAGTCCGATATTCTCGGCACCCGCGTTGAGCGCCCGGAAGTGCGCGAAGTCACC
GCATTGGGTGCGGCCTATCTCGCAGGCCTGGCGGTTGGCTTCTGGCAGAACCTCGACGAG
CTGCAAGAGAAAGCGGTGATTGAGCGCGAGTTCCGTCCAGGCATCGAAACCACTGAGCGT
AATTACCGTTACGCAGGCTGGAAAAAAGCGGTTAAACGCGCGATGGCGTGGGAAGAACAC
GACGAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A6F3
UniProtKB Entry NameGLPK_ECOLI
GenBank Protein ID146220
GenBank Gene IDM18393
General References
  1. Pettigrew DW, Ma DP, Conrad CA, Johnson JR: Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme. J Biol Chem. 1988 Jan 5;263(1):135-9. [Article]
  2. Weissenborn DL, Wittekindt N, Larson TJ: Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12. J Biol Chem. 1992 Mar 25;267(9):6122-31. [Article]
  3. Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Muramatsu S, Mizuno T: Nucleotide sequence of the region encompassing the glpKF operon and its upstream region containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 1989 Jun 12;17(11):4378. [Article]
  7. Gonzalez-Gil G, Bringmann P, Kahmann R: FIS is a regulator of metabolism in Escherichia coli. Mol Microbiol. 1996 Oct;22(1):21-9. [Article]
  8. Pettigrew DW, Liu WZ, Holmes C, Meadow ND, Roseman S: A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo. J Bacteriol. 1996 May;178(10):2846-52. [Article]
  9. Zwaig N, Lin EC: Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia coli. Science. 1966 Aug 12;153(3737):755-7. [Article]
  10. Hayashi SI, Lin EC: Purification and properties of glycerol kinase from Escherichia coli. J Biol Chem. 1967 Mar 10;242(5):1030-5. [Article]
  11. Thorner JW, Paulus H: Composition and subunit structure of glycerol kinase from Escherichia coli. J Biol Chem. 1971 Jun 25;246(12):3885-94. [Article]
  12. Thorner JW, Paulus H: Catalytic and allosteric properties of glycerol kinase from Escherichia coli. J Biol Chem. 1973 Jun 10;248(11):3922-32. [Article]
  13. de Riel JK, Paulus H: Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 1. Kinetic evidence. Biochemistry. 1978 Nov 28;17(24):5134-40. [Article]
  14. de Riel JK, Paulus H: Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidence. Biochemistry. 1978 Nov 28;17(24):5141-6. [Article]
  15. de Riel JK, Paulus H: Subunit dissociation in the allosteric regulation of Glycerol kinase from Escherichia coli. 3. Role in desensitization. Biochemistry. 1978 Nov 28;17(24):5146-50. [Article]
  16. Novotny MJ, Frederickson WL, Waygood EB, Saier MH Jr: Allosteric regulation of glycerol kinase by enzyme IIIglc of the phosphotransferase system in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1985 May;162(2):810-6. [Article]
  17. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  18. Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y: The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. doi: 10.1074/mcp.M111.012658. Epub 2011 Sep 9. [Article]
  19. Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ: Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Science. 1993 Jan 29;259(5095):673-7. [Article]
  20. Feese M, Pettigrew DW, Meadow ND, Roseman S, Remington SJ: Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3544-8. [Article]
  21. Ormo M, Bystrom CE, Remington SJ: Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate. Biochemistry. 1998 Nov 24;37(47):16565-72. [Article]
  22. Feese MD, Faber HR, Bystrom CE, Pettigrew DW, Remington SJ: Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Structure. 1998 Nov 15;6(11):1407-18. [Article]
  23. Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ: Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion. Biochemistry. 1999 Mar 23;38(12):3508-18. [Article]
  24. Anderson MJ, DeLabarre B, Raghunathan A, Palsson BO, Brunger AT, Quake SR: Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 --> Asp obtained using microfluidic crystallization devices. Biochemistry. 2007 May 15;46(19):5722-31. Epub 2007 Apr 19. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02937Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-DiphosphateexperimentalunknownDetails
DB04551beta-D-fructofuranose 1,6-bisphosphateexperimentalunknownDetails