twitter

MetaCyc Reaction: 3.6.4.4/3.6.4.5/3.6.4.6/3.6.4.7/3.6.4.8/3.6.4.9/3.6.4.10/3.6.4.11/3.6.4.12/3.6.4.13

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.6.4.4 , 3.6.4.5 , 3.6.4.6 , 3.6.4.7 , 3.6.4.8 , 3.6.4.9 , 3.6.4.10 , 3.6.4.11 , 3.6.4.12 , 3.6.4.13

Enzymes and Genes:

Aquifex aeolicus VF5 : nucleoside-triphosphatase Inferred from experiment : THEP1
Arabidopsis thaliana col : purple acid phosphatase [multifunctional] Inferred from experiment : PAP12
Bacillus subtilis subtilis 168 : nucleoside triphosphate phosphohydrolase : ytkD
Escherichia coli K-12 substr. MG1655 :
Glycine soja :
Homo sapiens :
Pisum sativum : nucleoside-triphosphatase : NTP1
Saccharomyces cerevisiae : apyrase : YND1
Solanum tuberosum : nucleoside triphosphate phosphohydrolase / ATP phosphohydrolase : RROP1

Sub-reaction of:
3.6.1.5: ATP + 2 H2O → AMP + 2 phosphate + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 3.6.4.4: plus-end-directed kinesin ATPase

Enzyme Commission Synonyms for 3.6.4.4: kinesin

Enzyme Commission Primary Name for 3.6.4.5: minus-end-directed kinesin ATPase

Enzyme Commission Primary Name for 3.6.4.6: vesicle-fusing ATPase

Enzyme Commission Primary Name for 3.6.4.7: peroxisome-assembly ATPase

Enzyme Commission Synonyms for 3.6.4.7: peroxisome assembly factor-2

Enzyme Commission Primary Name for 3.6.4.8: proteasome ATPase

Enzyme Commission Synonyms for 3.6.4.8: RP triple-A protein, RP triphosphatase

Enzyme Commission Primary Name for 3.6.4.9: chaperonin ATPase

Enzyme Commission Synonyms for 3.6.4.9: chaperonin

Enzyme Commission Primary Name for 3.6.4.10: non-chaperonin molecular chaperone ATPase

Enzyme Commission Synonyms for 3.6.4.10: molecular chaperone Hsc70 ATPase

Enzyme Commission Primary Name for 3.6.4.11: nucleoplasmin ATPase

Enzyme Commission Primary Name for 3.6.4.12: DNA helicase

Enzyme Commission Synonyms for 3.6.4.12: 3' to 5' DNA helicase, 3'-5' DNA helicase, 3'-5' PfDH, 5' to 3' DNA helicase, AvDH1, BACH1 helicase, BcMCM, BLM protein, BRCA1-associated C-terminal helicase, CeWRN-1, Dbp9p, DmRECQ5, DNA helicase 120, DNA helicase A, DNA helicase E, DNA helicase II, DNA helicase III, DNA helicase RECQL5β, DNA helicase VI, dnaB, DnaB helicase E1, helicase HDH IV, Hel E, helicase DnaB, helicase domain of bacteriophage T7 gene 4 protein helicase, UvrD, hHcsA, Hmi1p, hPif1, MCM helicase, MCM protein, MER3 helicase, MER3 protein, MPH1, PcrA, PcrA helicase, PDH120, PfDH A, Pfh1p, PIF1

Enzyme Commission Primary Name for 3.6.4.13: RNA helicase

Enzyme Commission Synonyms for 3.6.4.13: CSFV NS3 helicase, DBP2, DbpA, DDX17, DDX25, DDX3, DDX3X, DDX3Y, DDX4, DDX5, DEAD-box protein DED1, DEAD-box RNA helicase, DEAH-box protein 2, DEAH-box RNA helicase, DED1, Dex(H/D) RNA helicase, EhDEAD1, EhDEAD1 RNA helicase, eIF4A helicase, KOKV helicase, Mtr4p, nonstructural protein 3 helicase, NPH-II, RHA, RNA helicase A, RNA helicase DDX3, RNA helicase Hera, RNA-dependent ATPase, TGBp1 NTPase/helicase domain, VRH1, GRTH/DDX25

Taxonomic Range: Archaea , Viridiplantae , Bacteria , Fungi , Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -7.598877 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 3.6.4.4:
Microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (α) chains (110 kDa) and two or more light (β) chains (65-75 kDa). Also hydrolyses GTP.

Enzyme Commission Summary for 3.6.4.5:
Structurally almost identical to EC 3.6.4.4, plus-end-directed kinesin ATPase, but the movement it catalyzes is towards the minus end of microtubules.

Enzyme Commission Summary for 3.6.4.6:
A large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments.

They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily.

They include peroxin, which apparently is involved in Zellweger's syndrome.

Enzyme Commission Summary for 3.6.4.7:
An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle.

Their molecular masses range from 25 to 600 kDa.

Enzyme Commission Summary for 3.6.4.8:
Belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.

Enzyme Commission Summary for 3.6.4.9:
Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or to entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa.

Enzyme Commission Summary for 3.6.4.10:
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins.

They comprise a number of heat-shock-cognate proteins.

They are also active in clathrin uncoating and in the oligomerization of actin.

Enzyme Commission Summary for 3.6.4.11:
An acidic nuclear protein that is active in the ATP-dependent assembly of nucleosome cores, in decondensation of sperm chromatin and in other histone-involving processes.

Enzyme Commission Summary for 3.6.4.12:
DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. Some of them unwind duplex DNA with a 3 to 5 polarity [Ozsoy01, Nakagawa01, Phan03, Curti07], others show 5 to 3 polarity [Ivanov04, Ivessa02, Zhou02, George09] or unwind DNA in both directions [Naqvi03, RuizMaso06]. Some helicases unwind DNA as well as RNA [Frick07, Ivanov04]. May be identical with EC 3.6.4.13, RNA helicase.

Enzyme Commission Summary for 3.6.4.13:
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3 to 5 polarity [Lee92b], other show 5 to 3 polarity. Some helicases unwind DNA as well as RNA [Frick07]. May be identical with EC 3.6.4.12, DNA helicase.

Citations: [Vale85, Howard97, Nakagawa97, Henningsen97, Sharp97, Sablin98, Babst98, Imamura98, Confalonieri95, Lee92c, Tsukamoto95, Yahraus96, Rivett97, Mason98, Lubben89, Hemmingsen88, Ranson98, Sadis92, BlondElguindi93, Wawrzynow95, Sriram97, Li98, Laskey93, Cote94, Ito96a, Pike09, Bernstein03a, Lee98a, Tanner03, Cordin04, Rodamilans07, Li01, Wu05c, Gross98]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [a nucleoside triphosphate + H2O → a nucleoside diphosphate + phosphate + H+] (3.6.1.15):
i1: ATP + H2O → ADP + phosphate + H+ (3.6.4.4/3.6.4.5/3.6.4.6/3.6.4.7/3.6.4.8/3.6.4.9/3.6.4.10/3.6.4.11/3.6.4.12/3.6.4.13)

Unification Links: KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , Rhea:13065 , Rhea:13065

Relationship Links: BRENDA:EC:3.6.4.4 , BRENDA:EC:3.6.4.5 , BRENDA:EC:3.6.4.6 , BRENDA:EC:3.6.4.7 , BRENDA:EC:3.6.4.8 , BRENDA:EC:3.6.4.9 , BRENDA:EC:3.6.4.10 , BRENDA:EC:3.6.4.11 , BRENDA:EC:3.6.4.12 , BRENDA:EC:3.6.4.13 , ENZYME:EC:3.6.4.4 , ENZYME:EC:3.6.4.5 , ENZYME:EC:3.6.4.6 , ENZYME:EC:3.6.4.7 , ENZYME:EC:3.6.4.8 , ENZYME:EC:3.6.4.9 , ENZYME:EC:3.6.4.10 , ENZYME:EC:3.6.4.11 , ENZYME:EC:3.6.4.12 , ENZYME:EC:3.6.4.13 , IUBMB-ExplorEnz:EC:3.6.4.4 , IUBMB-ExplorEnz:EC:3.6.4.5 , IUBMB-ExplorEnz:EC:3.6.4.6 , IUBMB-ExplorEnz:EC:3.6.4.7 , IUBMB-ExplorEnz:EC:3.6.4.8 , IUBMB-ExplorEnz:EC:3.6.4.9 , IUBMB-ExplorEnz:EC:3.6.4.10 , IUBMB-ExplorEnz:EC:3.6.4.11 , IUBMB-ExplorEnz:EC:3.6.4.12 , IUBMB-ExplorEnz:EC:3.6.4.13 , UniProt:RELATED-TO:O24875 , UniProt:RELATED-TO:O27798 , UniProt:RELATED-TO:O51558 , UniProt:RELATED-TO:O51774 , UniProt:RELATED-TO:O66605 , UniProt:RELATED-TO:O67325 , UniProt:RELATED-TO:O83110 , UniProt:RELATED-TO:O83536 , UniProt:RELATED-TO:O84115 , UniProt:RELATED-TO:O84288 , UniProt:RELATED-TO:O84348 , UniProt:RELATED-TO:P02563 , UniProt:RELATED-TO:P02564 , UniProt:RELATED-TO:P02566 , UniProt:RELATED-TO:P02567 , UniProt:RELATED-TO:P03018 , UniProt:RELATED-TO:P05444 , UniProt:RELATED-TO:P05659 , UniProt:RELATED-TO:P08716 , UniProt:RELATED-TO:P08799 , UniProt:RELATED-TO:P0A9M0 , UniProt:RELATED-TO:P0A522 , UniProt:RELATED-TO:P0ABH9 , UniProt:RELATED-TO:P10568 , UniProt:RELATED-TO:P10569 , UniProt:RELATED-TO:P10587 , UniProt:RELATED-TO:P11055 , UniProt:RELATED-TO:P12844 , UniProt:RELATED-TO:P12845 , UniProt:RELATED-TO:P12847 , UniProt:RELATED-TO:P12883 , UniProt:RELATED-TO:P13533 , UniProt:RELATED-TO:P13535 , UniProt:RELATED-TO:P14105 , UniProt:RELATED-TO:P17422 , UniProt:RELATED-TO:P19524 , UniProt:RELATED-TO:P19706 , UniProt:RELATED-TO:P23098 , UniProt:RELATED-TO:P23596 , UniProt:RELATED-TO:P23787 , UniProt:RELATED-TO:P24428 , UniProt:RELATED-TO:P24733 , UniProt:RELATED-TO:P31539 , UniProt:RELATED-TO:P31540 , UniProt:RELATED-TO:P31541 , UniProt:RELATED-TO:P31542 , UniProt:RELATED-TO:P32492 , UniProt:RELATED-TO:P34036 , UniProt:RELATED-TO:P34092 , UniProt:RELATED-TO:P34109 , UniProt:RELATED-TO:P35100 , UniProt:RELATED-TO:P35579 , UniProt:RELATED-TO:P35580 , UniProt:RELATED-TO:P36022 , UniProt:RELATED-TO:P36773 , UniProt:RELATED-TO:P36774 , UniProt:RELATED-TO:P36775 , UniProt:RELATED-TO:P36776 , UniProt:RELATED-TO:P37276 , UniProt:RELATED-TO:P37571 , UniProt:RELATED-TO:P37945 , UniProt:RELATED-TO:P38650 , UniProt:RELATED-TO:P39057 , UniProt:RELATED-TO:P42762 , UniProt:RELATED-TO:P43864 , UniProt:RELATED-TO:P44403 , UniProt:RELATED-TO:P45443 , UniProt:RELATED-TO:P45444 , UniProt:RELATED-TO:P46067 , UniProt:RELATED-TO:P46523 , UniProt:RELATED-TO:P47481 , UniProt:RELATED-TO:P47807 , UniProt:RELATED-TO:P49574 , UniProt:RELATED-TO:P51332 , UniProt:RELATED-TO:P55995 , UniProt:RELATED-TO:P63284 , UniProt:RELATED-TO:P63288 , UniProt:RELATED-TO:P70704 , UniProt:RELATED-TO:P71404 , UniProt:RELATED-TO:P74361 , UniProt:RELATED-TO:P74459 , UniProt:RELATED-TO:P77810 , UniProt:RELATED-TO:P78025 , UniProt:RELATED-TO:P93647 , UniProt:RELATED-TO:Q7M4G4 , UniProt:RELATED-TO:Q9I8A2 , UniProt:RELATED-TO:Q9WY41 , UniProt:RELATED-TO:Q9X1B1 , UniProt:RELATED-TO:Q9X1W8 , UniProt:RELATED-TO:Q9Z8A6 , UniProt:RELATED-TO:Q9Z9F4 , UniProt:RELATED-TO:Q9ZD92 , UniProt:RELATED-TO:Q9ZEA9 , UniProt:RELATED-TO:Q9ZJL3 , UniProt:RELATED-TO:Q9ZMH1 , UniProt:RELATED-TO:Q9ZN31 , UniProt:RELATED-TO:Q09769 , UniProt:RELATED-TO:Q14204 , UniProt:RELATED-TO:Q16864 , UniProt:RELATED-TO:Q24368 , UniProt:RELATED-TO:Q27803 , UniProt:RELATED-TO:Q39575 , UniProt:RELATED-TO:Q55023 , UniProt:RELATED-TO:Q55662 , UniProt:RELATED-TO:Q59185 , UniProt:RELATED-TO:Q90909 , UniProt:RELATED-TO:Q90913 , UniProt:RELATED-TO:Q99323 , UniProt:RELATED-TO:Q9IBD4 , UniProt:RELATED-TO:Q9NTI2 , UniProt:RELATED-TO:Q9UKX2 , UniProt:RELATED-TO:Q9UMJ0 , UniProt:RELATED-TO:Q9UQV1 , UniProt:RELATED-TO:Q01989 , UniProt:RELATED-TO:Q02015 , UniProt:RELATED-TO:Q07443 , UniProt:RELATED-TO:Q28699 , UniProt:RELATED-TO:Q29449 , UniProt:RELATED-TO:Q39889 , UniProt:RELATED-TO:Q53368 ... [4 more not displayed]

Credits:
Created 22-Dec-2009 by Kothari A , SRI International


References

Babst98: Babst M, Wendland B, Estepa EJ, Emr SD (1998). "The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function." EMBO J 17(11);2982-93. PMID: 9606181

Bernstein03a: Bernstein DA, Zittel MC, Keck JL (2003). "High-resolution structure of the E.coli RecQ helicase catalytic core." EMBO J 22(19);4910-21. PMID: 14517231

BlondElguindi93: Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJ (1993). "Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers." J Biol Chem 268(17);12730-5. PMID: 8509407

Confalonieri95: Confalonieri F, Duguet M (1995). "A 200-amino acid ATPase module in search of a basic function." Bioessays 17(7);639-50. PMID: 7646486

Cordin04: Cordin O, Tanner NK, Doere M, Linder P, Banroques J (2004). "The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity." EMBO J 23(13);2478-87. PMID: 15201868

Cote94: Cote J, Quinn J, Workman JL, Peterson CL (1994). "Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex." Science 265(5168);53-60. PMID: 8016655

Curti07: Curti E, Smerdon SJ, Davis EO (2007). "Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD." J Bacteriol 189(5);1542-55. PMID: 17158674

Frick07: Frick DN (2007). "The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target." Curr Issues Mol Biol 9(1);1-20. PMID: 17263143

George09: George T, Wen Q, Griffiths R, Ganesh A, Meuth M, Sanders CM (2009). "Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks." Nucleic Acids Res 37(19);6491-502. PMID: 19700773

Gross98: Gross CH, Shuman S (1998). "The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication." J Virol 72(6);4729-36. PMID: 9573237

Hemmingsen88: Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly." Nature 333(6171);330-4. PMID: 2897629

Henningsen97: Henningsen U, Schliwa M (1997). "Reversal in the direction of movement of a molecular motor." Nature 389(6646);93-6. PMID: 9288974

Howard97: Howard J (1997). "Molecular motors: structural adaptations to cellular functions." Nature 389(6651);561-7. PMID: 9335494

Imamura98: Imamura A, Tamura S, Shimozawa N, Suzuki Y, Zhang Z, Tsukamoto T, Orii T, Kondo N, Osumi T, Fujiki Y (1998). "Temperature-sensitive mutation in PEX1 moderates the phenotypes of peroxisome deficiency disorders." Hum Mol Genet 7(13);2089-94. PMID: 9817926

Ito96a: Ito T, Tyler JK, Bulger M, Kobayashi R, Kadonaga JT (1996). "ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster." J Biol Chem 271(40);25041-8. PMID: 8798787

Ivanov04: Ivanov KA, Ziebuhr J (2004). "Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5'-triphosphatase activities." J Virol 78(14);7833-8. PMID: 15220459

Ivessa02: Ivessa AS, Zhou JQ, Schulz VP, Monson EK, Zakian VA (2002). "Saccharomyces Rrm3p, a 5' to 3' DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA." Genes Dev 16(11);1383-96. PMID: 12050116

Laskey93: Laskey RA, Mills AD, Philpott A, Leno GH, Dilworth SM, Dingwall C (1993). "The role of nucleoplasmin in chromatin assembly and disassembly." Philos Trans R Soc Lond B Biol Sci 339(1289);263-9; discussion 268-9. PMID: 8098530

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lee92b: Lee CG, Hurwitz J (1992). "A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3' to 5' direction." J Biol Chem 267(7);4398-407. PMID: 1537828

Lee92c: Lee YJ, Wickner RB (1992). "AFG1, a new member of the SEC18-NSF, PAS1, CDC48-VCP, TBP family of ATPases." Yeast 8(9);787-90. PMID: 1441755

Lee98a: Lee C, Seo YS (1998). "Isolation and characterization of a processive DNA helicase from the fission yeast Schizosaccharomyces pombe that translocates in a 5'-to-3' direction." Biochem J 334 ( Pt 2);377-86. PMID: 9716495

Li01: Li SC, Chung MC, Chen CS (2001). "Cloning and characterization of a DEAD box RNA helicase from the viable seedlings of aged mung bean." Plant Mol Biol 47(6);761-70. PMID: 11785937

Li98: Li X, Su RT, Hsu HT, Sze H (1998). "The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings." Plant Cell 10(1);119-30. PMID: 9477575

Lubben89: Lubben TH, Donaldson GK, Viitanen PV, Gatenby AA (1989). "Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone." Plant Cell 1(12);1223-30. PMID: 2577724

Mason98: Mason GG, Murray RZ, Pappin D, Rivett AJ (1998). "Phosphorylation of ATPase subunits of the 26S proteasome." FEBS Lett 430(3);269-74. PMID: 9688553

Nakagawa01: Nakagawa T, Flores-Rozas H, Kolodner RD (2001). "The MER3 helicase involved in meiotic crossing over is stimulated by single-stranded DNA-binding proteins and unwinds DNA in the 3' to 5' direction." J Biol Chem 276(34);31487-93. PMID: 11376001

Nakagawa97: Nakagawa T, Tanaka Y, Matsuoka E, Kondo S, Okada Y, Noda Y, Kanai Y, Hirokawa N (1997). "Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome." Proc Natl Acad Sci U S A 94(18);9654-9. PMID: 9275178

Naqvi03: Naqvi A, Tinsley E, Khan SA (2003). "Purification and characterization of the PcrA helicase of Bacillus anthracis." J Bacteriol 185(22);6633-9. PMID: 14594837

Ozsoy01: Ozsoy AZ, Sekelsky JJ, Matson SW (2001). "Biochemical characterization of the small isoform of Drosophila melanogaster RECQ5 helicase." Nucleic Acids Res 29(14);2986-93. PMID: 11452023

Phan03: Phan TN, Ehtesham NZ, Tuteja R, Tuteja N (2003). "A novel nuclear DNA helicase with high specific activity from Pisum sativum catalytically translocates in the 3'-->5' direction." Eur J Biochem 270(8);1735-45. PMID: 12694186

Pike09: Pike AC, Shrestha B, Popuri V, Burgess-Brown N, Muzzolini L, Costantini S, Vindigni A, Gileadi O (2009). "Structure of the human RECQ1 helicase reveals a putative strand-separation pin." Proc Natl Acad Sci U S A 106(4);1039-44. PMID: 19151156

Ranson98: Ranson NA, White HE, Saibil HR (1998). "Chaperonins." Biochem J 333 ( Pt 2);233-42. PMID: 9657960

Rivett97: Rivett AJ, Mason GG, Murray RZ, Reidlinger J (1997). "Regulation of proteasome structure and function." Mol Biol Rep 24(1-2);99-102. PMID: 9228289

Rodamilans07: Rodamilans B, Montoya G (2007). "Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain." Acta Crystallogr Sect F Struct Biol Cryst Commun 63(Pt 4);283-6. PMID: 17401195

RuizMaso06: Ruiz-Maso JA, Anand SP, Espinosa M, Khan SA, del Solar G (2006). "Genetic and biochemical characterization of the Streptococcus pneumoniae PcrA helicase and its role in plasmid rolling circle replication." J Bacteriol 188(21);7416-25. PMID: 16936036

Sablin98: Sablin EP, Case RB, Dai SC, Hart CL, Ruby A, Vale RD, Fletterick RJ (1998). "Direction determination in the minus-end-directed kinesin motor ncd." Nature 395(6704);813-6. PMID: 9796817

Sadis92: Sadis S, Hightower LE (1992). "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange." Biochemistry 31(39);9406-12. PMID: 1356434

Sharp97: Sharp DJ, Kuriyama R, Essner R, Baas PW (1997). "Expression of a minus-end-directed motor protein induces Sf9 cells to form axon-like processes with uniform microtubule polarity orientation." J Cell Sci 110 ( Pt 19);2373-80. PMID: 9410876

Sriram97: Sriram M, Osipiuk J, Freeman B, Morimoto R, Joachimiak A (1997). "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain." Structure 5(3);403-14. PMID: 9083109

Tanner03: Tanner JA, Watt RM, Chai YB, Lu LY, Lin MC, Peiris JS, Poon LL, Kung HF, Huang JD (2003). "The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases." J Biol Chem 278(41);39578-82. PMID: 12917423

Tsukamoto95: Tsukamoto T, Miura S, Nakai T, Yokota S, Shimozawa N, Suzuki Y, Orii T, Fujiki Y, Sakai F, Bogaki A, Yasumo H, Osumi T (1995). "Peroxisome assembly factor-2, a putative ATPase cloned by functional complementation on a peroxisome-deficient mammalian cell mutant." Nat Genet 11(4);395-401. PMID: 7493019

Vale85: Vale RD, Reese TS, Sheetz MP (1985). "Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility." Cell 42(1);39-50. PMID: 3926325

Wawrzynow95: Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M (1995). "The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone." EMBO J 14(9);1867-77. PMID: 7743994

Wu05c: Wu J, Bera AK, Kuhn RJ, Smith JL (2005). "Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing." J Virol 79(16);10268-77. PMID: 16051820

Yahraus96: Yahraus T, Braverman N, Dodt G, Kalish JE, Morrell JC, Moser HW, Valle D, Gould SJ (1996). "The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor." EMBO J 15(12);2914-23. PMID: 8670792

Zhou02: Zhou JQ, Qi H, Schulz VP, Mateyak MK, Monson EK, Zakian VA (2002). "Schizosaccharomyces pombe pfh1+ encodes an essential 5' to 3' DNA helicase that is a member of the PIF1 subfamily of DNA helicases." Mol Biol Cell 13(6);2180-91. PMID: 12058079


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Tue May 5, 2015, BIOCYC14A.