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13  structures 311  species 2  interactions 1160  sequences 22  architectures

Family: 6PF2K (PF01591)

Summary: 6-phosphofructo-2-kinase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "6-phosphofructo-2-kinase". More...

6-phosphofructo-2-kinase Edit Wikipedia article

6-phosphofructo-2-kinase
Identifiers
EC number 2.7.1.105
CAS number 78689-77-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
6PF2K
PDB 1k6m EBI.jpg
crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Identifiers
Symbol 6PF2K
Pfam PF01591
Pfam clan CL0023
InterPro IPR013079
PROSITE PDOC00158
SCOP 1bif
SUPERFAMILY 1bif

In enzymology, a 6-phosphofructo-2-kinase (EC 2.7.1.105) is an enzyme that catalyzes the chemical reaction

ATP + beta-D-fructose 6-phosphate \rightleftharpoons ADP + beta-D-fructose 2,6-bisphosphate

Thus, the two substrates of this enzyme are ATP and beta-D-fructose 6-phosphate, whereas its two products are ADP and beta-D-fructose 2,6-bisphosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:beta-D-fructose-6-phosphate 2-phosphotransferase. Other names in common use include phosphofructokinase 2, 6-phosphofructose 2-kinase, 6-phosphofructo-2-kinase (phosphorylating), fructose 6-phosphate 2-kinase, and ATP:D-fructose-6-phosphate 2-phosphotransferase. This enzyme participates in fructose and mannose metabolism. The enzyme is important in the regulation of hepatic carbohydrate metabolism and is found in greatest quantities in the liver, kidney and heart. In mammals, several genes often encode different isoforms, each of which differs in its tissue distribution and enzymatic activity.[1] The family described here bears a resemblance to the ATP-driven phospho-fructokinases, however, they share little sequence similarity, although a few residues seem key to their interaction with fructose 6-phosphate.[2]

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1BIF, 1K6M, 2AXN, 2BIF, 2DWO, 2DWP, 2I1V, and 3BIF.

References

  1. ^ Heine-Suñer D, Díaz-Guillén MA, Lange AJ, Rodríguez de Córdoba S (May 1998). "Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)". Eur. J. Biochem. 254 (1): 103–10. doi:10.1046/j.1432-1327.1998.2540103.x. PMID 9652401. 
  2. ^ Wang X, Deng Z, Kemp RG (September 1998). "An essential methionine residue involved in substrate binding by phosphofructokinases". Biochem. Biophys. Res. Commun. 250 (2): 466–8. doi:10.1006/bbrc.1998.9311. PMID 9753654. 
  • Van Schaftingen E, Hers HG (1981). "Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP". Biochem. Biophys. Res. Commun. 101 (3): 1078–84. doi:10.1016/0006-291X(81)91859-3. PMID 6458291. 

This article incorporates text from the public domain Pfam and InterPro IPR013079


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Phosphofructokinase 2". More...

Phosphofructokinase 2 Edit Wikipedia article

6-phosphofructo-2-kinase
Identifiers
EC number 2.7.1.105
CAS number 78689-77-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
fructose-2,6-bisphosphate 2-phosphatase
Identifiers
EC number 3.1.3.46
CAS number 81611-75-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
6-phosphofructo-2-kinase
Phosphofructokinase 2.jpg
Structure of PFK2. Shown: kinase domain (cyan) and the phosphatase domain (green).
Identifiers
Symbol 6PF2K
Pfam PF01591
InterPro IPR013079
PROSITE PDOC00158
SCOP 1bif
SUPERFAMILY 1bif

Phosphofructokinase 2 (PFK2) or fructose bisphosphatase 2 (FBPase2), is an enzyme responsible for regulating the rates of glycolysis and gluconeogenesis in the human body. It is a homodimer of 55 kDa subunits arranged in a head-to-head fashion, with each polypeptide chain consisting of independent kinase and phosphatase domain. When Ser-32 of the bifunctional protein is phosphorylated, the negative charge causes the conformation change of the enzyme to favor the FBPase2 activity; otherwise, PFK2 activity is favored.[1] PFK2 domain is closely related to the superfamily of mononucleotide binding proteins including adenylate cyclase, whereas that of FBPase2 is related to a family of proteins that include phosphoglycerate mutases.

Structure

The monomers of the bifunctional protein are clearly divided into two functional domains. The kinase domain is located on the N-terminal.[2] It consists of a central six-stranded β sheet, with five parallel strands and an antiparallel edge strand, surrounded by seven α helices.[3] The domain contains nucleotide-binding fold (nbf) at the C-terminal end of the first β-strand,[4] and thus resembles the structure of adenylate kinase.

On the other hand, the phosphatase domain is located on the C-terminal.[5] It resembles the family of proteins that include phosphoglycerate mutases (PGMs) and acid phosphatases.[6] The domain has a mixed α/ β structure, with a six-stranded central β sheet, plus an additional α-helical subdomain that covers the presumed active site of the molecule.[3] Finally, N-terminal region modulates PFK2 and FBPase2 activities, and stabilizes the dimer form of the enzyme.[6][7]

Function

When glucose level is low, glucagon is released into the bloodstream, triggering a cAMP signal cascade. In the liver Protein kinase A inactivates the PFK-2 domain of the bifunctional enzyme via phosphorylation, however this does not occur in skeletal muscle. The F-2,6-BPase domain is then activated which lowers fructose 2,6-bisphosphate (F-2,6-BP) levels. Because F-2,6-BP normally stimulates phosphofructokinase-1(PFK1), the decrease in its concentration leads to the inhibition of glycolysis and the stimulation of gluconeogenesis.[8]

On the other hand, when the glucose level increases, the level of fructose 6-phosphate (F6P) subsequently rises and the molecule stimulates phosphoprotein phosphatase-1, which removes phosphoryl group from the bifunctional protein. So PFK2 domain is activated and the kinase catalyzes the formation of F-2,6-BP. Thus, glycolysis is stimulated and gluconeogenesis is inhibited.

Regulation

The allosteric regulation of PFK2 is very similar to the regulation of PFK1.[9] High levels of AMP or phosphate group signifies high levels of glucose and thus stimulates PFK2. On the other hand, a high concentration of phosphoenolpyruvate(PEP) and citrate signifies that there is a high level of biosynthetic precursor and hence inhibits PFK2. However, unlike PFK1, PFK2 is not affected by the ATP concentration.

Glucagon inhibits PFK2 by activating Protein Kinase A (PKA), which phosphorylates the PFK2 complex and causes its FBPase activity to be favored; via PKA and PFK2/FBP, glucagon decreases [F-2,6-BP], which inhibits glycolysis by allosteric inhibition of PFK1. Insulin activates PFK2 by activating Protein Phosphatase, which dephosphorylates the PFK-2 complex and causes its PFK2 activity to be favored; via Protein Phosphatase and PFK2, insulin increases [F-2,6-BP], which activates glycolysis by allosteric activation of PFK1.

Reaction mechanism

PFK2 is likely to catalyze the "simple" transfer of γ-phosphoryl group of ATP onto the hydroxyl present on C-2 of fructose-6-phosphate. Yet, the formation of fructose 2,6-bisphosphate could theoretically occur by a variety of mechanisms, including the intermediary formation of Fructose-6-phosphate 2-pyrophosphate.[9]

The hydrolysis of fructose 2,6-biphosphate is likely to follow the below steps:[10]

  1. Histidine acts as a nucleophile and attacks the 2-phosphate of F-2,6-BP
  2. The stabilization of pentacoordinated transition state by several salt bridges and hydrogen bonding.
  3. The breakdown of the transition state and the release of F6P.
  4. Histidine increases the nucleophilicity of water, which attacks phosphohistidine, generating phosphate and newly protonated histidine.

Clinical significance

The Pfkfb2 gene encoding PFK2/FBPase2 protein is linked to the predisposition to schizophrenia.[11] Furthermore, the control of PFK2/FBPase2 activity was found to be linked to heart functioning and the control against hypoxia.[12]

Isozymes

Five mammalian isozymes of the protein have been reported to date, difference rising by either the transcription of different enzymes or alternative splicing.[13][14][15]The isozymes differ radically in their regulation and the discussions above are based on liver isozyme.[3]

Humans genes encoding proteins possessing phosphofructokinase 2 activity include:

References

  1. ^ Kurland IJ, el-Maghrabi MR, Correia JJ, Pilkis SJ (March 1992). "Rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Properties of phospho- and dephospho- forms and of two mutants in which Ser32 has been changed by site-directed mutagenesis". J. Biol. Chem. 267 (7): 4416–23. PMID 1339450. 
  2. ^ Kurland I, Chapman B, Lee YH, Pilkis S (August 1995). "Evolutionary reengineering of the phosphofructokinase active site: ARG-104 does not stabilize the transition state in 6-phosphofructo-2-kinase". Biochem. Biophys. Res. Commun. 213 (2): 663–72. doi:10.1006/bbrc.1995.2183. PMID 7646523. 
  3. ^ a b c Hasemann CA, Istvan ES, Uyeda K, Deisenhofer J (September 1996). "The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies". Structure 4 (9): 1017–29. doi:10.1016/S0969-2126(96)00109-8. PMID 8805587. 
  4. ^ Walker JE, Saraste M, Runswick MJ, Gay NJ (1982). "Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold". EMBO J. 1 (8): 945–51. PMC 553140. PMID 6329717. 
  5. ^ Li L, Lin K, Pilkis J, Correia JJ, Pilkis SJ (October 1992). "Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. The role of surface loop basic residues in substrate binding to the fructose-2,6-bisphosphatase domain". J. Biol. Chem. 267 (30): 21588–94. PMID 1328239. 
  6. ^ a b Stryer, Lubert; Berg, Jeremy Mark; Tymoczko, John L. (2008). "The Balance Between Glycolysis and Gluconeogenesis in the Liver Is Sensitive to Blood-Glucose Concentration". Biochemistry (Looseleaf). San Francisco: W. H. Freeman. pp. 466–467. ISBN 1-4292-3502-0. 
  7. ^ Tominaga N, Minami Y, Sakakibara R, Uyeda K (July 1993). "Significance of the amino terminus of rat testis fructose-6-phosphate, 2-kinase:fructose-2,6-bisphosphatase". J. Biol. Chem. 268 (21): 15951–7. PMID 8393455. 
  8. ^ Pilkis SJ, Claus TH, Kurland IJ, Lange AJ (1995). "6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase: a metabolic signaling enzyme". Annu. Rev. Biochem. 64: 799–835. doi:10.1146/annurev.bi.64.070195.004055. PMID 7574501. 
  9. ^ a b Van Schaftingen E, Hers HG (August 1981). "Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP". Biochem. Biophys. Res. Commun. 101 (3): 1078–84. doi:10.1016/0006-291X(81)91859-3. PMID 6458291. 
  10. ^ Lin K, Li L, Correia JJ, Pilkis SJ (April 1992). "Glu327 is part of a catalytic triad in rat liver fructose-2,6-bisphosphatase". J. Biol. Chem. 267 (10): 6556–62. PMID 1313012. 
  11. ^ Stone WS, Faraone SV, Su J, Tarbox SI, Van Eerdewegh P, Tsuang MT (May 2004). "Evidence for linkage between regulatory enzymes in glycolysis and schizophrenia in a multiplex sample". Am. J. Med. Genet. B Neuropsychiatr. Genet. 127B (1): 5–10. doi:10.1002/ajmg.b.20132. PMID 15108172. 
  12. ^ Wang Q, Donthi RV, Wang J, Lange AJ, Watson LJ, Jones SP, Epstein PN (June 2008). "Cardiac phosphatase-deficient 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase increases glycolysis, hypertrophy, and myocyte resistance to hypoxia". Am. J. Physiol. Heart Circ. Physiol. 294 (6): H2889–97. doi:10.1152/ajpheart.91501.2007. PMID 18456722. 
  13. ^ Darville MI, Crepin KM, Hue L, Rousseau GG (September 1989). "5' flanking sequence and structure of a gene encoding rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase". Proc. Natl. Acad. Sci. U.S.A. 86 (17): 6543–7. doi:10.1073/pnas.86.17.6543. PMC 297880. PMID 2549541. 
  14. ^ Tsuchiya Y, Uyeda K (May 1994). "Bovine heart fructose 6-P,2-kinase:fructose 2,6-bisphosphatase mRNA and gene structure". Arch. Biochem. Biophys. 310 (2): 467–74. doi:10.1006/abbi.1994.1194. PMID 8179334. 
  15. ^ Sakata J, Abe Y, Uyeda K (August 1991). "Molecular cloning of the DNA and expression and characterization of rat testes fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase". J. Biol. Chem. 266 (24): 15764–70. PMID 1651918. 

Further reading

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

6-phosphofructo-2-kinase Provide feedback

This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyses both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis [1]. This enzyme contains a P-loop motif.

Literature references

  1. Hasemann CA, Istvan ES, Uyeda K, Deisenhofer J; , Structure 1996;4:1017-1029.: The crystal structure of the bifunctional enzyme 6-phosphofructo-2- kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies. PUBMED:8805587 EPMC:8805587


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013079

6-Phosphofructo-2-kinase (EC, EC) is a bifunctional enzyme that catalyses both the synthesis and the degradation of fructose-2, 6-bisphosphate. The fructose-2,6-bisphosphatase reaction involves a phosphohistidine intermediate. The catalytic pathway is: ATP + D-fructose 6-phosphate = ADP + D-fructose 2,6-bisphosphate D-fructose 2,6-bisphosphate + H2O = 6-fructose 6-phosphate + Pi The enzyme is important in the regulation of hepatic carbohydrate metabolism and is found in greatest quantities in the liver, kidney and heart. In mammals, several genes often encode different isoforms, each of which differs in its tissue distribution and enzymatic activity [PUBMED:9652401]. The family described here bears a resemblance to the ATP-driven phospho-fructokinases, however, they share little sequence similarity, although a few residues seem key to their interaction with fructose 6-phosphate [PUBMED:9753654].

This domain forms the N-terminal region of this enzyme, while INTERPRO forms the C-terminal domain.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan P-loop_NTPase (CL0023), which has the following description:

AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].

The clan contains the following 198 members:

6PF2K AAA AAA-ATPase_like AAA_10 AAA_11 AAA_12 AAA_13 AAA_14 AAA_15 AAA_16 AAA_17 AAA_18 AAA_19 AAA_2 AAA_21 AAA_22 AAA_23 AAA_24 AAA_25 AAA_26 AAA_27 AAA_28 AAA_29 AAA_3 AAA_30 AAA_31 AAA_32 AAA_33 AAA_34 AAA_35 AAA_4 AAA_5 AAA_6 AAA_7 AAA_8 AAA_9 AAA_PrkA ABC_ATPase ABC_tran ABC_tran_2 Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arch_ATPase Arf ArgK ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 Bac_DnaA CbiA CMS1 CoaE CobA_CobO_BtuR CobU cobW CPT CTP_synth_N Cytidylate_kin Cytidylate_kin2 DAP3 DEAD DEAD_2 DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DNA_pol3_delta2 DnaB_C dNK DUF1253 DUF1611 DUF2075 DUF2478 DUF258 DUF2791 DUF2813 DUF3584 DUF463 DUF815 DUF853 DUF87 DUF927 Dynamin_N Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GTP_EFTU GTP_EFTU_D2 GTP_EFTU_D4 Gtr1_RagA Guanylate_kin GvpD HDA2-3 Helicase_C Helicase_C_2 Helicase_C_4 Helicase_RecD Herpes_Helicase Herpes_ori_bp Herpes_TK IIGP IPPT IPT IstB_IS21 KaiC KAP_NTPase Kinesin Kinesin-relat_1 Kinesin-related KTI12 LpxK MCM MEDS Mg_chelatase Mg_chelatase_2 MipZ Miro MMR_HSR1 MobB MukB MutS_V Myosin_head NACHT NB-ARC NOG1 NTPase_1 ParA Parvo_NS1 PAXNEB PduV-EutP PhoH PIF1 Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK Rad17 Rad51 Ras RecA ResIII RHD3 RHSP RNA12 RNA_helicase RuvB_N SbcCD_C SecA_DEAD Septin Sigma54_activ_2 Sigma54_activat SKI SMC_N SNF2_N Spore_IV_A SRP54 SRPRB Sulfotransfer_1 Sulfotransfer_2 Sulfotransfer_3 Sulphotransf T2SE T4SS-DNA_transf Terminase_1 Terminase_3 Terminase_6 Terminase_GpA Thymidylate_kin TIP49 TK TniB Torsin TraG-D_C tRNA_lig_kinase TrwB_AAD_bind UPF0079 UvrD-helicase UvrD_C UvrD_C_2 Viral_helicase1 VirC1 VirE YhjQ Zeta_toxin Zot

Alignments

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(351)
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Representative proteomes NCBI
(1195)
Meta
(96)
RP15
(187)
RP35
(351)
RP55
(557)
RP75
(696)
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  Seed
(11)
Full
(1160)
Representative proteomes NCBI
(1195)
Meta
(96)
RP15
(187)
RP35
(351)
RP55
(557)
RP75
(696)
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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_717 (release 4.1)
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 11
Number in full: 1160
Average length of the domain: 194.90 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 39.97 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 20.8 20.8
Noise cut-off 20.7 20.7
Model length: 223
Family (HMM) version: 13
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Species distribution

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Interactions

There are 2 interactions for this family. More...

6PF2K His_Phos_1

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the 6PF2K domain has been found. There are 13 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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