Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: glycerol kinase



Gene: glpK Accession Numbers: EG10398 (EcoCyc), b3926, ECK3918

Regulation Summary Diagram: ?

Subunit composition of glycerol kinase = [GlpK]4

Summary:
Glycerol kinase (GlpK) is involved in the utilization of the glycerol moiety of phospholipids and triglycerides after their breakdown into usable forms such as glycerophosphodiesters, sn-glycerol-3-phosphate (G3P) or glycerol. GlpK catalyzes the MgATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate [Lin76]. This reaction is the rate limiting step in glycerol utilization and is dependent on added divalent cation [Zwaig70, Thorner75, Hayashi67]. GlpK is a member of a superfamily of ATPases that share a common ATPase domain [Pettigrew88, Bork92].

GlpK is associated with a glycerol faciliator (GlpF) and together are involved with the entry of external glycerol into cellular metabolism. GlpF provides a selective channel while GlpK traps the glycerol inside the cell [Voegele93, Weissenborn92].

GlpK is an important regulatory enzyme in glucose control of glycerol metabolism and is subject to inhibition by fructose 1,6-bisphosphate (FBP) and the nonphosphorylated form of enzyme IIIGlc [Zwaig66, Novotny85]. FBP is the dominant allosteric effector since glucose is unable to control glycerol utilization in its absence [Holtman01]. GlpK also seems to be regulated by adenine nucleotides [Pettigrew86].

The enzyme can undergo a reversible subunit dissociation between tetramer and dimer [deRiel78].

The 3D structure of GlpK has been extensively studied. [Faber89, Bystrom99, Mao99]. The crystal structure of GlpK in complex with unphosphorylated IIIGlc, glycerol and ADP was determined at 2.6 Å resolution [Hurley93]. Various mutants of GlpK have been crystallized [Feese98, Anderson07a]. The crystal structure of GlpK with bound glycerol in the presence and absence of one FBP has also been determined [Ormo98].

Mutations in glpK affect catalytic function and regulation as well as reduce affinity and inhibition by FBP and IIIGlc [Pettigrew09, Applebee11, Liu94b, Pettigrew96].

Gene Citations: [Lupski90, Truniger92]

Locations: cytosol

Map Position: [4,113,737 <- 4,115,245] (88.66 centisomes)
Length: 1509 bp / 502 aa

Molecular Weight of Polypeptide: 56.231 kD (from nucleotide sequence), 55.0 kD (experimental) [Thorner71 ]

Molecular Weight of Multimer: 217.0 kD (experimental) [Thorner71]

pI: 5.58

Unification Links: ASAP:ABE-0012825 , CGSC:691 , DIP:DIP-36011N , EchoBASE:EB0393 , EcoGene:EG10398 , EcoliWiki:b3926 , OU-Microarray:b3926 , PortEco:glpK , Pride:P0A6F3 , Protein Model Portal:P0A6F3 , RefSeq:NP_418361 , RegulonDB:EG10398 , SMR:P0A6F3 , String:511145.b3926 , UniProt:P0A6F3

Relationship Links: InterPro:IN-FAMILY:IPR005999 , InterPro:IN-FAMILY:IPR018483 , InterPro:IN-FAMILY:IPR018484 , InterPro:IN-FAMILY:IPR018485 , Panther:IN-FAMILY:PTHR10196:SF9 , PDB:Structure:1BO5 , PDB:Structure:1BOT , PDB:Structure:1BU6 , PDB:Structure:1BWF , PDB:Structure:1GLA , PDB:Structure:1GLB , PDB:Structure:1GLC , PDB:Structure:1GLD , PDB:Structure:1GLE , PDB:Structure:1GLF , PDB:Structure:1GLJ , PDB:Structure:1GLL , PDB:Structure:3EZW , Pfam:IN-FAMILY:PF00370 , Pfam:IN-FAMILY:PF02782 , Prosite:IN-FAMILY:PS00445 , Prosite:IN-FAMILY:PS00933

In Paralogous Gene Group: 21 (7 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006071 - glycerol metabolic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Hayashi67, Pettigrew96]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0016310 - phosphorylation Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Hayashi67]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [GOA01]
GO:0006072 - glycerol-3-phosphate metabolic process Inferred by computational analysis [GOA06, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0019563 - glycerol catabolic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004370 - glycerol kinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Hayashi67]
GO:0005515 - protein binding Inferred from experiment [Zheng11]
GO:0005524 - ATP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, Bystrom99]
GO:0008270 - zinc ion binding Inferred from experiment [Feese94]
GO:0042802 - identical protein binding Inferred from experiment [Thorner71]
GO:0046872 - metal ion binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Hayashi67]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016773 - phosphotransferase activity, alcohol group as acceptor Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]

MultiFun Terms: metabolism central intermediary metabolism misc. glycerol metabolism

Essentiality data for glpK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 3]

Credits:
Last-Curated ? 22-Oct-2013 by Kubo A , SRI International


Enzymatic reaction of: glycerol kinase

Synonyms: glycerokinase, ATP:glycerol 3-phosphotransferase, GK

EC Number: 2.7.1.30

glycerol + ATP <=> sn-glycerol 3-phosphate + ADP + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for glycerol [Hayashi67 ]: dihydroxyacetone [Hayashi67 ] , L-glyceraldehyde [Hayashi67 ]

In Pathways: glycerol and glycerophosphodiester degradation , glycerol degradation I

Cofactors or Prosthetic Groups [Comment 4]: Mg2+ [Pettigrew88]

Alternative Cofactors for Mg2+: Mn2+

Activators (Unknown Mechanism): ATP [Pettigrew90]

Inhibitors (Competitive): AMPPNP [Pettigrew90] , sn-glycerol 3-phosphate [Pettigrew90, Comment 5] , ADP [Helmward89, Comment 6]

Inhibitors (Noncompetitive): ADP [Thorner73] , fructose 1,6-bisphosphate (Ki = 500µM) [Thorner73]

Inhibitors (Unknown Mechanism): 5'-[p-(fluorosulphonyl)benzoyl]adenosine [Pettigrew88, Helmward89] , glycerol [Pettigrew90, Comment 7] , AMPPNP [Pettigrew90]

Primary Physiological Regulators of Enzyme Activity: fructose 1,6-bisphosphate

Kinetic Parameters:

Substrate
Km (μM)
Citations
glycerol
1.3
[Hayashi67]
ATP
7.8
[Applebee11, BRENDA14]
ATP
4000.0
[Hayashi67]

pH(opt): 9.8 [BRENDA14, Hayashi67]


Sequence Features

Feature Class Location Attached Group Citations Comment
Cleavage-of-Initial-Methionine 1  
[GonzalezGil96, UniProt11]
UniProt: Removed.
Chain 2 -> 502  
[UniProt09]
UniProt: Glycerol kinase;
Nucleotide-Phosphate-Binding-Region 14 -> 16 ATP
[UniProt14]
UniProt: ATP.
Amino-Acid-Sites-That-Bind 14  
[UniProt10]
UniProt: Substrate;
Amino-Acid-Sites-That-Bind 18  
[UniProt10]
UniProt: ATP;
Mutagenesis-Variant 59  
[UniProt14]
Alternate sequence: S → W; UniProt: Abolishes inhibition of GK by FBP via disruption of the dimer-tetramer assembly reaction. Inhibition by EIIA-Glc is unchanged compared to wild type. The activity of this mutant is significantly higher than wild-type, and the Michaelis constants are increased slightly compared to wild-type.
Mutagenesis-Variant 66  
[UniProt14]
Alternate sequence: A → T; UniProt: Although it completely abolishes FBP regulation and disruptes dimer- tetramer equilibrium, the crystal structure is essentially identical to the symmetric tetramer found in the FBP-bound form of the enzyme.
Protein-Segment 84 -> 85  
[UniProt14]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 136  
[UniProt10]
UniProt: Substrate;
Mutagenesis-Variant 231  
[UniProt14]
Alternate sequence: G → D; UniProt: Displays an increased enzymatic activity and a decreased allosteric regulation by FBP compared to wild-type. It displays a dimer form and is resistant to tetramer formation in the presence of FBP, whereas wild-type dimers are converted into inactive tetramers in the presence of FBP.
Modified-Residue 233  
[Peng11, UniProt12]
UniProt: N6-malonyllysine.
Protein-Segment 234 -> 236  
[UniProt14]
UniProt: Allosteric FBP inhibitor binding; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 237  
[UniProt14]
Alternate sequence: R → A; UniProt: Drastically reduces inhibition of GK by FBP and lowers, but did not eliminate, the ability of FBP to promote tetramer association.
Protein-Segment 246 -> 247  
[UniProt14]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 268  
[UniProt10]
UniProt: ATP;
Mutagenesis-Variant 305  
[UniProt10]
Alternate sequence: G → S; UniProt: In glpK22; abolishes glucose control of glycerol utilization;
Amino-Acid-Sites-That-Bind 311  
[UniProt10]
UniProt: ATP; via carbonyl oxygen;
Amino-Acid-Sites-That-Bind 315  
[UniProt14]
UniProt: ATP; via amide nitrogen.
Amino-Acid-Sites-That-Bind 330  
[UniProt14]
UniProt: ATP.
Nucleotide-Phosphate-Binding-Region 412 -> 416  
[UniProt10]
UniProt: ATP;
Mutagenesis-Variant 475  
[UniProt14]
Alternate sequence: I → D; UniProt: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. It increases the affinity for FBP about fivefold.
Metal-Binding-Site 479  
[UniProt10]
UniProt: Zinc; shared with EIIA-Glc;
Mutagenesis-Variant 480  
[UniProt14]
Alternate sequence: R → D; UniProt: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. Regulation by FBP is not affected by this substitution. No inhibition by EIIA-Glc is observed, which is consistent with a decrease in affinity for EIIA-Glc of about 250-fold.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3926 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10398; confirmed by SwissProt match.


References

Anderson07a: Anderson MJ, DeLabarre B, Raghunathan A, Palsson BO, Brunger AT, Quake SR (2007). "Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 --> Asp obtained using microfluidic crystallization devices." Biochemistry 46(19);5722-31. PMID: 17441732

Applebee11: Applebee MK, Joyce AR, Conrad TM, Pettigrew DW, Palsson BO (2011). "Functional and metabolic effects of adaptive glycerol kinase (GLPK) mutants in Escherichia coli." J Biol Chem 286(26);23150-9. PMID: 21550976

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bork92: Bork P, Sander C, Valencia A (1992). "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." Proc Natl Acad Sci U S A 89(16);7290-4. PMID: 1323828

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Bystrom99: Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ (1999). "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 38(12);3508-18. PMID: 10090737

deRiel78: de Riel JK, Paulus H (1978). "Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidence." Biochemistry 1978;17(24);5141-6. PMID: 215195

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Faber89: Faber HR, Pettigrew DW, Remington SJ (1989). "Crystallization and preliminary X-ray studies of Escherichia coli glycerol kinase." J Mol Biol 207(3);637-9. PMID: 2547969

Feese94: Feese M, Pettigrew DW, Meadow ND, Roseman S, Remington SJ (1994). "Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation." Proc Natl Acad Sci U S A 91(9);3544-8. PMID: 8170944

Feese98: Feese MD, Faber HR, Bystrom CE, Pettigrew DW, Remington SJ (1998). "Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation." Structure 6(11);1407-18. PMID: 9817843

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

GonzalezGil96: Gonzalez-Gil G, Bringmann P, Kahmann R (1996). "FIS is a regulator of metabolism in Escherichia coli." Mol Microbiol 22(1);21-9. PMID: 8899705

Hayashi67: Hayashi SI, Lin EC (1967). "Purification and properties of glycerol kinase from Escherichia coli." J Biol Chem 1967;242(5);1030-5. PMID: 5335908

Helmward89: Helmward Z "Handbook of Enzyme Inhibitors. 2nd, revised and enlarged edition." Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989.

Holtman01: Holtman CK, Pawlyk AC, Meadow ND, Pettigrew DW (2001). "Reverse genetics of Escherichia coli glycerol kinase allosteric regulation and glucose control of glycerol utilization in vivo." J Bacteriol 183(11);3336-44. PMID: 11344141

Hurley93: Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ (1993). "Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase." Science 259(5095);673-7. PMID: 8430315

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Lin76: Lin EC (1976). "Glycerol dissimilation and its regulation in bacteria." Annu Rev Microbiol 1976;30;535-78. PMID: 825019

Liu94b: Liu WZ, Faber R, Feese M, Remington SJ, Pettigrew DW (1994). "Escherichia coli glycerol kinase: role of a tetramer interface in regulation by fructose 1,6-bisphosphate and phosphotransferase system regulatory protein IIIglc." Biochemistry 33(33);10120-6. PMID: 8060980

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lupski90: Lupski JR, Zhang YH, Rieger M, Minter M, Hsu B, Ooi BG, Koeuth T, McCabe ER (1990). "Mutational analysis of the Escherichia coli glpFK region with Tn5 mutagenesis and the polymerase chain reaction." J Bacteriol 1990;172(10);6129-34. PMID: 2170343

Mao99: Mao C, Ozer Z, Zhou M, Uckun FM (1999). "X-Ray structure of glycerol kinase complexed with an ATP analog implies a novel mechanism for the ATP-dependent glycerol phosphorylation by glycerol kinase." Biochem Biophys Res Commun 259(3);640-4. PMID: 10364471

Novotny85: Novotny MJ, Frederickson WL, Waygood EB, Saier MH (1985). "Allosteric regulation of glycerol kinase by enzyme IIIglc of the phosphotransferase system in Escherichia coli and Salmonella typhimurium." J Bacteriol 162(2);810-6. PMID: 2985549

Ormo98: Ormo M, Bystrom CE, Remington SJ (1998). "Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate." Biochemistry 37(47);16565-72. PMID: 9843423

Peng11: 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 (2011). "The first identification of lysine malonylation substrates and its regulatory enzyme." Mol Cell Proteomics 10(12);M111.012658. PMID: 21908771

Pettigrew09: Pettigrew DW (2009). "Oligomeric interactions provide alternatives to direct steric modes of control of sugar kinase/actin/hsp70 superfamily functions by heterotropic allosteric effectors: inhibition of E. coli glycerol kinase." Arch Biochem Biophys 492(1-2);29-39. PMID: 19819219

Pettigrew86: Pettigrew DW (1986). "Inactivation of Escherichia coli glycerol kinase by 5,5'-dithiobis(2-nitrobenzoic acid) and N-ethylmaleimide: evidence for nucleotide regulatory binding sites." Biochemistry 25(16);4711-8. PMID: 3021201

Pettigrew88: Pettigrew DW, Ma DP, Conrad CA, Johnson JR (1988). "Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme." J Biol Chem 1988;263(1);135-9. PMID: 2826434

Pettigrew90: Pettigrew DW, Yu GJ, Liu Y (1990). "Nucleotide regulation of Escherichia coli glycerol kinase: initial-velocity and substrate binding studies." Biochemistry 1990;29(37);8620-7. PMID: 2148683

Pettigrew96: Pettigrew DW, Liu WZ, Holmes C, Meadow ND, Roseman S (1996). "A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo." J Bacteriol 178(10);2846-52. PMID: 8631672

Thorner71: Thorner JW, Paulus H (1971). "Composition and subunit structure of glycerol kinase from Escherichia coli." J Biol Chem 246(12);3885-94. PMID: 4934840

Thorner73: Thorner JW, Paulus H (1973). "Catalytic and allosteric properties of glycerol kinase from Escherichia coli." J Biol Chem 1973;248(11);3922-32. PMID: 4575199

Thorner75: Thorner JW (1975). "Glycerol kinase." Methods Enzymol 1975;42;148-56. PMID: 237175

Truniger92: Truniger V, Boos W, Sweet G (1992). "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri." J Bacteriol 174(21);6981-91. PMID: 1400248

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt12: UniProt Consortium (2012). "UniProt version 2012-09 released on 2012-09-12 00:00:00." Database.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-01 released on 2014-01-01 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Voegele93: Voegele RT, Sweet GD, Boos W (1993). "Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator." J Bacteriol 175(4);1087-94. PMID: 8432702

Weissenborn92: Weissenborn DL, Wittekindt N, Larson TJ (1992). "Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12." J Biol Chem 1992;267(9);6122-31. PMID: 1372899

Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552

Zwaig66: Zwaig N, Lin EC (1966). "Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia coli." Science 153(3737);755-7. PMID: 5328677

Zwaig70: Zwaig N, Kistler WS, Lin EC (1970). "Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli." J Bacteriol 1970;102(3);753-9. PMID: 4914079

Other References Related to Gene Regulation

Beisel12: Beisel CL, Updegrove TB, Janson BJ, Storz G (2012). "Multiple factors dictate target selection by Hfq-binding small RNAs." EMBO J 31(8);1961-74. PMID: 22388518

Zhang11h: Zhang Z, Saier MH (2011). "Transposon-mediated adaptive and directed mutations and their potential evolutionary benefits." J Mol Microbiol Biotechnol 21(1-2);59-70. PMID: 22248543


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, biocyc13.