MetaCyc Reaction:

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

EC Number: , , , , , , , , , , , , , , , , ,

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: ATP + 2 H2O → AMP + 2 phosphate + 2 H+

Supersedes EC numbers:,

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 adenosinetriphosphatase

Enzyme Commission Synonyms for adenylpyrophosphatase, ATP monophosphatase, triphosphatase, ATPase (ambiguous), SV40 T-antigen, adenosine 5'-triphosphatase, ATP hydrolase, complex V (mitochondrial electron transport), (Ca2+ + Mg2+)-ATPase, HCO3--ATPase, adenosine triphosphatase

Enzyme Commission Primary Name for nucleoside-triphosphate phosphatase

Enzyme Commission Synonyms for nucleoside-triphosphatase, nucleoside triphosphate phosphohydrolase, nucleoside-5-triphosphate phosphohydrolase, nucleoside 5-triphosphatase, unspecific diphosphate phosphohydrolase

Enzyme Commission Primary Name for protein-secreting ATPase

Enzyme Commission Primary Name for mitochondrial protein-transporting ATPase

Enzyme Commission Primary Name for chloroplast protein-transporting ATPase

Enzyme Commission Primary Name for myosin ATPase

Enzyme Commission Synonyms for Actomyosin

Enzyme Commission Primary Name for dynein ATPase

Enzyme Commission Synonyms for dynein adenosine 5'-triphosphatase

Enzyme Commission Primary Name for microtubule-severing ATPase

Enzyme Commission Synonyms for Katanin

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

Enzyme Commission Synonyms for kinesin

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

Enzyme Commission Primary Name for vesicle-fusing ATPase

Enzyme Commission Primary Name for peroxisome-assembly ATPase

Enzyme Commission Synonyms for peroxisome assembly factor-2

Enzyme Commission Primary Name for proteasome ATPase

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

Enzyme Commission Primary Name for chaperonin ATPase

Enzyme Commission Synonyms for chaperonin

Enzyme Commission Primary Name for non-chaperonin molecular chaperone ATPase

Enzyme Commission Synonyms for molecular chaperone Hsc70 ATPase

Enzyme Commission Primary Name for nucleoplasmin ATPase

Enzyme Commission Primary Name for DNA helicase

Enzyme Commission Synonyms for 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 RNA helicase

Enzyme Commission Synonyms for 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
Many enzymes previously listed under this number are now listed separately under EC 3.6.3 and EC 3.6.4.

Enzyme Commission Summary for
Also hydrolyses other nucleoside triphosphates, diphosphates, thiamine diphosphate and FAD.

Enzyme Commission Summary for
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport.

There are several families of enzymes included here, e.g. ATP-hydrolyzing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV).

Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.

Enzyme Commission Summary for
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex.

TIM is the protein transport machinery of the inner mitochondrial membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat- shock protein Hsp70 to form an ATP-driven import motor.

Enzyme Commission Summary for
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport.

Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).

Enzyme Commission Summary for
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.

Enzyme Commission Summary for
A multisubunit protein complex associated with microtubules. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome towards the microtubule's minus end. It also functions in the movement of eukaryotic flagella and cilia. It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa).

Enzyme Commission Summary for
Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.

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

Enzyme Commission Summary for
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
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
Belongs to the AAA-type superfamily and, like EC, 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
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
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
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
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, RNA helicase.

Enzyme Commission Summary for
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3 to 5 polarity [Lee92a], other show 5 to 3 polarity. Some helicases unwind DNA as well as RNA [Frick07]. May be identical with EC, DNA helicase.

Citations: [Martin80, Geider81, Riley81, Tjian81, Matsushita68, Lewis65, Brightwell68, Tong93, Hsieh96, Klinger03, Placzek07, Saier94, Mecsas, Thomas97, Baker97, Martinez98, Schuch99, Bomer97, Berthold95, Voos99, Cline92, Nakai94, Scott96, Rayment96, Hasson96, Murphy99a, Gibbons88, Summers71, Gee98, McNally93, Hartman98, Vale85, Howard97, Nakagawa97, Henningsen97, Sharp97, Sablin98, Babst98, Imamura98, Confalonieri95, Lee92b, Tsukamoto95, Yahraus96, Rivett97, Mason98, Lubben89, Hemmingsen88, Ranson98, Sadis92, BlondElguindi93, Wawrzynow95, Sriram97, Li98, Laskey93, Cote94, Ito96, Pike09, Bernstein03, Lee98, Tanner03, Cordin04, Rodamilans07, Li01, Wu05a, Gross98]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [a nucleoside triphosphate + H2O → a nucleoside diphosphate + phosphate + H+] (
i1: ATP + H2O → ADP + phosphate + H+ (

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: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , BRENDA:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , IUBMB-ExplorEnz:EC: , 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 ... [28 more not displayed]

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


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

Baker97: Baker B, Zambryski P, Staskawicz B, Dinesh-Kumar SP (1997). "Signaling in plant-microbe interactions." Science 276(5313);726-33. PMID: 9115193

Bernstein03: 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

Berthold95: Berthold J, Bauer MF, Schneider HC, Klaus C, Dietmeier K, Neupert W, Brunner M (1995). "The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system." Cell 81(7);1085-93. PMID: 7600576

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

Bomer97: Bomer U, Meijer M, Maarse AC, Honlinger A, Dekker PJ, Pfanner N, Rassow J (1997). "Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane." EMBO J 16(9);2205-16. PMID: 9171336

Brightwell68: Brightwell R, Tappel AL (1968). "Lysosomal acid pyrophosphatase and acid phosphatase." Arch Biochem Biophys 124(1);333-43. PMID: 5661608

Cline92: Cline K, Ettinger WF, Theg SM (1992). "Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP." J Biol Chem 267(4);2688-96. PMID: 1733965

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

Gee98: Gee M, Vallee R (1998). "The role of the dynein stalk in cytoplasmic and flagellar motility." Eur Biophys J 27(5);466-73. PMID: 9760728

Geider81: Geider K, Hoffmann-Berling H (1981). "Proteins controlling the helical structure of DNA." Annu Rev Biochem 50;233-60. PMID: 6267987

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

Gibbons88: Gibbons IR (1988). "Dynein ATPases as microtubule motors." J Biol Chem 263(31);15837-40. PMID: 2972702

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

Hartman98: Hartman JJ, Mahr J, McNally K, Okawa K, Iwamatsu A, Thomas S, Cheesman S, Heuser J, Vale RD, McNally FJ (1998). "Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit." Cell 93(2);277-87. PMID: 9568719

Hasson96: Hasson T, Mooseker MS (1996). "Vertebrate unconventional myosins." J Biol Chem 271(28);16431-4. PMID: 8690736

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

Hsieh96: Hsieh HL, Tong CG, Thomas C, Roux SJ (1996). "Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea." Plant Mol Biol 30(1);135-47. PMID: 8616230

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

Ito96: 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

Klinger03: Klinger C, Rossbach M, Howe R, Kaufmann M (2003). "Thermophile-specific proteins: the gene product of aq_1292 from Aquifex aeolicus is an NTPase." BMC Biochem 4;12. PMID: 14503925

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."

Lee92a: 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

Lee92b: 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

Lee98: 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

Lewis65: Lewis M, Weissman S (1965). "Properties of a soluble nucleoside triphosphatase activity in mammalian liver." Arch Biochem Biophys 109;490-8. PMID: 14320490

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

Martin80: Martin SS, Senior AE (1980). "Membrane adenosine triphosphatase activities in rat pancreas." Biochim Biophys Acta 602(2);401-18. PMID: 6252965

Martinez98: Martinez A, Ostrovsky P, Nunn DN (1998). "Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion." Mol Microbiol 28(6);1235-46. PMID: 9680212

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

Matsushita68: Matsushita S, Raacke ID (1968). "Purification of nucleoside triphosphatases from pea seedling ribosomes." Biochim Biophys Acta 166(3);707-10. PMID: 4301913

McNally93: McNally FJ, Vale RD (1993). "Identification of katanin, an ATPase that severs and disassembles stable microtubules." Cell 75(3);419-29. PMID: 8221885

Mecsas: Mecsas JJ, Strauss EJ "Molecular mechanisms of bacterial virulence: type III secretion and pathogenicity islands." Emerg Infect Dis 2(4);270-88. PMID: 8969244

Murphy99a: Murphy CT, Spudich JA (1999). "The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity." Biochemistry 38(12);3785-92. PMID: 10090768

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

Nakai94: Nakai M, Goto A, Nohara T, Sugita D, Endo T (1994). "Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport." J Biol Chem 269(50);31338-41. PMID: 7989297

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

Placzek07: Placzek WJ, Almeida MS, Wuthrich K (2007). "NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase." J Mol Biol 367(3);788-801. PMID: 17291528

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

Rayment96: Rayment I (1996). "The structural basis of the myosin ATPase activity." J Biol Chem 271(27);15850-3. PMID: 8663496

Riley81: Riley MV, Peters MI (1981). "The localization of the anion-sensitive ATPase activity in corneal endothelium." Biochim Biophys Acta 644(2);251-6. PMID: 6114746

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

Saier94: Saier MH, Tam R, Reizer A, Reizer J (1994). "Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport." Mol Microbiol 11(5);841-7. PMID: 8022262

Schuch99: Schuch R, Maurelli AT (1999). "The mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasin translocation." Infect Immun 67(4);1982-91. PMID: 10085046

Scott96: Scott SV, Theg SM (1996). "A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implications." J Cell Biol 132(1-2);63-75. PMID: 8567731

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

Summers71: Summers KE, Gibbons IR (1971). "Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm." Proc Natl Acad Sci U S A 68(12);3092-6. PMID: 5289252

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

Thomas97: Thomas JD, Reeves PJ, Salmond GP (1997). "The general secretion pathway of Erwinia carotovora subsp. carotovora: analysis of the membrane topology of OutC and OutF." Microbiology 143 ( Pt 3);713-20. PMID: 9084158

Tjian81: Tjian R (1981). "Regulation of viral transcription and DNA replication by the SV40 large T antigen." Curr Top Microbiol Immunol 93;5-24. PMID: 6269805

Tong93: Tong CG, Dauwalder M, Clawson GA, Hatem CL, Roux SJ (1993). "The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins." Plant Physiol 101(3);1005-11. PMID: 7508630

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

Voos99: Voos W, Martin H, Krimmer T, Pfanner N (1999). "Mechanisms of protein translocation into mitochondria." Biochim Biophys Acta 1422(3);235-54. PMID: 10548718

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

Wu05a: 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

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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