Information on EC 3.1.3.35 - thymidylate 5'-phosphatase:
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The enzyme appears in viruses and cellular organisms

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EC NUMBERCOMMENTARY
3.1.3.35-

RECOMMENDED NAMEGeneOntology No.
thymidylate 5'-phosphataseGO:0050340

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
thymidylate + H2O = thymidine + phosphate
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysis of phosphoric ester----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
thymidylate 5'-phosphohydrolaseActs on 5-methyl-dCMP and on TMP, but more slowly than on dTMP.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
deoxythymidylate 5'-nucleotidase----
deoxythymidylate phosphohydrolase----
deoxythymidylic 5'-nucleotidase----
dTMPase----
nucleotidase, thymidylate----
thymidylate 5'-nucleotidase----

CAS REGISTRY NUMBERCOMMENTARY
9026-80-6-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bacillus phage PBS2expression in Brevibacterium helvolum650698--Manually annotated by BRENDA team
Bacillus subtilisinfected with phage PBS281085, 81086--Manually annotated by BRENDA team
Bacillus subtilisSB19, infected with phage SP5C81084--Manually annotated by BRENDA team
Bos taurusPDE6652211--Manually annotated by BRENDA team
Bos taurus PDE6PDE6652211--Manually annotated by BRENDA team
Homo sapiens-650791--Manually annotated by BRENDA team
Mesocricetus auratus-81087--Manually annotated by BRENDA team
Mus musculus-81088--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2'-fluoro-dTMP + H2O2'-fluorodeoxythymidine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
2-thio-dTMP + H2O2-thiodeoxythymidine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
4-thio-dTMP + H2O4-thiodeoxythymidine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
5-ethyl-dUMP + H2O5-ethyldeoxyuridine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
5-methylamino-dUMP + H2O5-methylaminodeoxyuridine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
6-aza-dTMP + H2O6-azadeoxythymidine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
arabino-TMP + H2Oarabino-thymidine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
deoxy-5-methyl-CMP + phosphatedeoxy-5-methylcytidine + phosphate
show the reaction diagram		Bacillus subtilis--81084-81084-
deoxythymidine 5'-phosphate + H2Odeoxythymidine + phosphate
show the reaction diagram		Bacillus subtilis--81084-81084?
deoxythymidine 5'-phosphate + H2Odeoxythymidine + phosphate
show the reaction diagram		Bacillus subtilis--81085, 81086--?
deoxythymidine 5'-phosphate + H2Odeoxythymidine + phosphate
show the reaction diagram		Mus musculus--81088--?
deoxythymidine 5'-phosphate + H2Odeoxythymidine + phosphate
show the reaction diagram		Mesocricetus auratus--81087--?
dGMP + H2Odeoxyguanosine + phosphate
show the reaction diagram		Bacillus subtilis--81084---
dGMP + H2Odeoxyguanosine + phosphate
show the reaction diagram		Bacillus subtilis--81085--?
dTMp + H2OdT + phosphate
show the reaction diagram		Homo sapiens--650791-650791?
dTMP + H2Othymidine + phosphate
show the reaction diagram		Bacillus subtilis--81084, 81086---
dTMP + H2Othymidine + phosphate
show the reaction diagram		Bacillus subtilis-functions to hydrolyze dTMP and thus to prevent accumulation of dTTP in the cell during phage infection81085---
ribo-TMP + H2Oribo-thymidine + phosphate
show the reaction diagram		Bacillus subtilis--81086--?
dUMP + H2Odeoxyuridine + phosphate
show the reaction diagram		Bacillus subtilis--81085, 81086--?
additional information?-Homo sapiens-substrate cycle between thymidine and thymidylate in exponentially growing cells, regulation of enzyme650791-650791?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
dTMP + H2Othymidine + phosphate
show the reaction diagram		Bacillus subtilis-functions to hydrolyze dTMP and thus to prevent accumulation of dTTP in the cell during phage infection81085--
additional information?-Homo sapiens-substrate cycle between thymidine and thymidylate in exponentially growing cells, regulation of enzyme650791-650791

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Bacillus subtilis-can substitute for Mg2+ in activation81085
Mg2+Bacillus subtilis-activation, optimal concentration 8 mM81084
Mg2+Bacillus subtilis-Km: 0.06 mM81085
Mg2+Bacillus subtilis--81086
Mn2+Bacillus subtilis-activation, optimal concentration 0.4 mM, inhibition above81084
Ni2+Bacillus subtilis-can substitute for Mg2+ in activation81085

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
5,5'-dithiobis(2-nitrobenzoate)Bacillus subtilis--81086 2D-image
ChloramphenicolBacillus subtilis-inhibits the synthesis of the enzyme81084 2D-image
Cu2+Bacillus subtilis--81085, 81086 2D-image
dTMPBacillus subtilis--81086 2D-image
EDTABacillus subtilis--81084 2D-image
F-Bacillus subtilis--81084, 81086 2D-image
Hg2+Bacillus subtilis--81085, 81086 2D-image
KClBacillus subtilis--81086 2D-image
LiClBacillus subtilis--81086 2D-image
Mn2+Bacillus subtilis-inhibition above 0.4 mM81084 2D-image
NaClBacillus subtilis--81086 2D-image
p-hydroxymercuribenzoateBacillus subtilis--81086 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
6-deoxy-5-methyl-CMPBacillus subtilis--81084 2D-image
0.7-dGMPBacillus subtilis--81084 2D-image
0.01-dTMPBacillus subtilis--81085, 81086 2D-image
1-dTMPBacillus subtilis--81084 2D-image
73.39-dTMPHomo sapiens-pH 7.5, 37°C, exponentially growing cells650791 2D-image
1267-dTMPHomo sapiens-pH 7.5, 37°C, stationary phase cells650791 2D-image
0.8-dUMPBacillus subtilis--81085, 81086 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
113-Bacillus subtilis--81085

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5.86.8Bacillus subtilis--81085, 81086
6.9-Bacillus subtilis--81084

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
6.47.8Bacillus subtilis-80% of maximal activity at pH 6.4, 42% of maximal activity at pH 7.8, no activity at pH 6.081084

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
37-Bacillus subtilis-substrate dUMP81086
37-Mesocricetus auratus--81087
42-Bacillus subtilis--81085
42-Bacillus subtilis-substrate dTMP81086

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
CHO cellMesocricetus auratus--81087Manually annotated by BRENDA team
Ehrlich ascites carcinoma cellHomo sapiens--650791Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
additional informationBos taurus-relation of membrane-associated and soluble enzyme depends on light response-652211Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
40000-Bacillus subtilis-gel filtration81085

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional informationBos taurus-delta subunit modifies the activity of the phototransduction cascade652211

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
4.510.5Bacillus subtilis-inactivated above pH 10.5 and below pH 4.581085, 81086

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
52-Bacillus subtilis-50% inactivation in 3 min81086

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°C, partially purified, 50% glycerol, at least 1 year with loss of activityBacillus subtilis-81086

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
partialBacillus subtilis-81084, 81085, 81086

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
biotechnologyBacillus phage PBS2-production of thymidine by expression of enzyme in a Brevibacteruium helvolum mutant resistant to fluorouracil, hydroxyurea, trimethoprim650698

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
InfectionA DTMPASE FOUND AFTER INFECTION OF BACILLUS SUBTILIS WITH PHAGE SP5C. PubMed
InfectionDeoxythymidylate 5'-nucleotidase. Purification and properties of an enzyme found after infection of Bacillus subtilis with phage SP5C. PubMed
InfectionDeoxythymidylate phosphohydrolase induced by bacteriophage PBS2 during infection of Bacillus subtilis. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
81084Vasken Aposhian, H.; Tremblay, G.Y.Deoxythymidylate 5-nucleotidase. Purification and properties of an enzyme found after infection of Bacillus subtilis with phage SP5CJ. Biol. Chem.2415095-51011966Bacillus subtilis PubMed
81085Price, A.R.Deoxythymidylate phosphohydrolase from PBS2 phage-infected Bacillus subtilisMethods Enzymol.51285-2901978Bacillus subtilis PubMed
81086Price, A.R.; Fogt, S.M.Deoxythymidylate phosphohydrolase induced by bacteriophage PBS2 during infection of Bacillus subtilisJ. Biol. Chem.2481372-13801973Bacillus subtilis PubMed
81087Schaer, J.C.; Maurer, U.Thymidine nucleotide synthesis and catabolism by CHO cells and their changes during the cell cycleBiochim. Biophys. Acta697221-2281982Mesocricetus auratus PubMed
81088Fisher, S.E.; Dawe, C.; Williams, J.E.; DeWard Morgan, W.Isozyme phenotypes of polyoma virus tumors in miceCancer Res.433783-37921983Mus musculus PubMed
650698Lee, H.C.; Ahn, J.M.; Lee, S.N.; Kim, J.H.Overproduction of thymidine by recombinant Brevibacterium helvolum amplified with thymidine monophosphate phosphohydrolase gene from bacteriophage PBS2Biotechnol. Lett.26265-2682004Bacillus phage PBS2 PubMed
650791He, Q.; Skog, S.Involvement of a substrate cycle between thymidine and thymidylate in the regulation of DNA precursor pool in Ehrlich ascites tumorCell. Physiol. Biochem.12305-3142002Homo sapiens PubMed
652211Cook, T.A.; Ghomashchi, F.; Gelb, M.H.; Florio, S.K.; Beavo, J.A.The delta subunit of type 6 phosphodiesterase reduces light-induced cGMP hydrolysis in rod outer segmentsJ. Biol. Chem.2765248-52552001Bos taurus PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 3.1.3.35)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)