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Escherichia coli K-12 substr. MG1655 Enzyme: purine nucleoside phosphorylase



Gene: deoD Accession Numbers: EG10222 (EcoCyc), b4384, ECK4376

Synonyms: pup

Regulation Summary Diagram: ?

Subunit composition of purine nucleoside phosphorylase = [DeoD]6
         purine nucleoside phosphorylase = DeoD

Summary:
DeoD (also called PNP-I) is one of the two purine nuceloside phosphorylases (PNPs) in E. coli. PNPs use orthophosphate to cleave the N-glycosidic bond of the β-(deoxy)ribonucleosides to produce α-(deoxy)ribose1-phosphate and the free purine base. The bases can be utilized as precursors in the synthesis of nucleotides in the purine and pyrimidine salvage pathways as well as a nitrogen source. The pentose-1-phosphate formed serves as a carbon source. The other PNP, PNP-II xanthosine phosphorylase, differ in substrate specificity. DeoD is a homohexamer and has broader substrate specificity but cannot act on xanthosine [ModrakWojcik08] [Dandanell05][Jensen75]. Additionally, DeoD can catalyze a phosphate-dependent transfer of the pentose moiety from one purine base to another [Jensen75].

Phosphate stimulates the ribosyl transferase activity, and kinetic studies show strong negative cooperativity in binding of phosphate to the enzyme [Jensen75]. The reaction mechanism has been explored [Jensen76]. The enzyme is inhibited by Cu2+ and Zn2+ [Bezirdzhian87]. Reports differ on whether ([Bezirdzhian87]) or not ([Jensen75]) Ni2+ and SO42- inhibit the enzyme.

Crystal structures of DeoD have been determined for wild-type and mutant enzymes and their complexes with substrate analogs. The catalytic mechanisms and substrate specificities of the enzymes were analyzed [Mao97a, Koellner98, Koellner02, Bennett03a, Bennett03b, Mikleuševi11].

Due to structural differences between the E. coli and the human enzymes, potential therapeutic approaches using the E. coli enzyme have prompted studies of its mechanism of action and determinants of its activity. The use of E. coli PNP in suicide gene therapy against tumors has been explored; for reviews, see [Zhang05f, Bzowska00]. More recent approaches are described in [Parker11, Li10c]. In addition, the reverse (nucleoside synthesis) reaction and the transglycosylation reaction of DeoD can be utilized in the production of nucleosides and nucleoside derivatives for drug development [Ding10, Ge09].

Expression of purine nucleoside phosphorylase is induced by growth in the presence of purine and pyrimidine deoxyribonucleosides [Rachmeler61] as well as inosine and guanosine [HammerJespersen71].

A deoD mutant can not grow on adenosine or deoxyadenosine as the sole source of carbon [Buxton75].

The enzyme is a member of the nucleoside phosphorylase -I family [Pugmire02].

Pup: "purine nucleoside phosphorylase" [Ahmad68]

DeoD: "deoxyribonucleoside" [Lomax68]

Reviews: Jensen, K.F., G. Dandanell, B. Hove-Jensen, and M. Willemoes (2008) "Nucleotides, Nucleosides and Nucleobases" EcoSal 3.6.2 [ECOSAL]] and [Pugmire02, Zhang05f, Bzowska00]

Gene Citations: [ValentinHansen84, Albrechtsen80, Svenningsen75]

Locations: membrane, cytosol

Map Position: [4,618,906 -> 4,619,625] (99.55 centisomes)
Length: 720 bp / 239 aa

Molecular Weight of Polypeptide: 25.95 kD (from nucleotide sequence), 23.7 kD (experimental) [Jensen75 ]

Molecular Weight of Multimer: 150 kD (experimental) [ModrakWojcik06]

pI: 5.69

Unification Links: ASAP:ABE-0014379 , CGSC:865 , DIP:DIP-36195N , EchoBASE:EB0218 , EcoGene:EG10222 , EcoliWiki:b4384 , Entrez-gene:945654 , Mint:MINT-8328110 , ModBase:P0ABP8 , OU-Microarray:b4384 , PortEco:deoD , PR:PRO_000022430 , Pride:P0ABP8 , Protein Model Portal:P0ABP8 , RefSeq:NP_418801 , RegulonDB:EG10222 , SMR:P0ABP8 , String:511145.b4384 , UniProt:P0ABP8

Relationship Links: InterPro:IN-FAMILY:IPR000845 , InterPro:IN-FAMILY:IPR004402 , InterPro:IN-FAMILY:IPR018016 , InterPro:IN-FAMILY:IPR018017 , Panther:IN-FAMILY:PTHR21234 , PDB:Structure:1A69 , PDB:Structure:1ECP , PDB:Structure:1K9S , PDB:Structure:1OTX , PDB:Structure:1OTY , PDB:Structure:1OU4 , PDB:Structure:1OUM , PDB:Structure:1OV6 , PDB:Structure:1OVG , PDB:Structure:3ONV , PDB:Structure:3OOE , PDB:Structure:3OOH , PDB:Structure:3OPV , PDB:Structure:3UT6 , Pfam:IN-FAMILY:PF01048 , Prosite:IN-FAMILY:PS01232

In Paralogous Gene Group: 588 (2 members)

Gene-Reaction Schematic: ?

Instance reactions of [a purine ribonucleoside + phosphate ↔ a purine base + α-D-ribose-1-phosphate] (2.4.2.1):
i1: adenosine + phosphate ↔ α-D-ribose-1-phosphate + adenine (2.4.2.1)

i2: inosine + phosphate ↔ α-D-ribose-1-phosphate + hypoxanthine (2.4.2.1)

i3: guanosine + phosphate ↔ α-D-ribose-1-phosphate + guanine (2.4.2.1/2.4.2.15)

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006152 - purine nucleoside catabolic process Inferred from experiment [Buxton75]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0019686 - purine nucleoside interconversion Inferred from experiment [Jensen75]
GO:0006139 - nucleobase-containing compound metabolic process Inferred by computational analysis [GOA01a]
GO:0009116 - nucleoside metabolic process Inferred by computational analysis [GOA01a]
GO:0042278 - purine nucleoside metabolic process Inferred by computational analysis [GOA06]
Molecular Function: GO:0004731 - purine-nucleoside phosphorylase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Jensen75]
GO:0042802 - identical protein binding Inferred from experiment [Bertosa14, ŠtefaniZ12, Lasserre06, Jensen75]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016757 - transferase activity, transferring glycosyl groups Inferred by computational analysis [UniProtGOA11a]
GO:0016763 - transferase activity, transferring pentosyl groups Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]

MultiFun Terms: metabolism carbon utilization
metabolism central intermediary metabolism nucleotide and nucleoside conversions

Essentiality data for deoD 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 Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Curated 12-Dec-2006 by Keseler I , SRI International
Reviewed 08-Feb-2010 by Sarker M
Last-Curated ? 02-Dec-2011 by Fulcher C , SRI International


Enzymatic reaction of: guanosine phosphorylase (purine nucleoside phosphorylase)

EC Number: 2.4.2.1

guanosine + phosphate <=> α-D-ribose-1-phosphate + guanine

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

This reaction is reversible.

Alternative Substrates for guanosine: 1-methylguanosine [Bzowska88 ]

In Pathways: superpathway of guanine and guanosine salvage , guanine and guanosine salvage , guanosine nucleotides degradation III , purine ribonucleosides degradation

Kinetic Parameters:

Substrate
Km (μM)
Citations
guanosine
20.0
[Bzowska88]


Enzymatic reaction of: purine nucleoside phosphorylase

Synonyms: inosine phosphorylase, PNP, purine-nucleoside:orthophosphate ribosyltransferase

EC Number: 2.4.2.1

a purine ribonucleoside + phosphate <=> a purine base + α-D-ribose-1-phosphate

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

This reaction is reversible.

Alternative Substrates [Comment 5]:

In Pathways: superpathway of guanine and guanosine salvage , guanine and guanosine salvage , guanosine nucleotides degradation III , adenosine nucleotides degradation II , adenine and adenosine salvage III , adenine and adenosine salvage V , purine ribonucleosides degradation


Enzymatic reaction of: deoxyguanosine phosphorylase (purine nucleoside phosphorylase)

EC Number: 2.4.2.1

2'-deoxyguanosine + phosphate <=> guanine + 2-deoxy-α-D-ribose 1-phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

In Pathways: superpathway of purine deoxyribonucleosides degradation , purine deoxyribonucleosides degradation I

Inhibitors (Competitive): adenosine [Bezirdzhian86]

Kinetic Parameters:

Substrate
Km (μM)
Citations
2'-deoxyguanosine
98.5
[Bezirdzhian86]


Enzymatic reaction of: inosine phosphorylase (purine nucleoside phosphorylase)

EC Number: 2.4.2.1

inosine + phosphate <=> α-D-ribose-1-phosphate + hypoxanthine

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

This reaction is reversible. [Jensen75]

Alternative Substrates for inosine: 1-methylinosine [Bzowska88 ]

In Pathways: adenosine nucleotides degradation II , adenine and adenosine salvage III , purine ribonucleosides degradation

Summary:
The pH optimun for phosphorolysis is 7.5, while the pH optimum for the ribosyl transferase activity is 8.2 [Jensen75]. The equilibrium constant of the reaction at 25 °C, defined as [inosine][H2PO4-] / [hypoxanthine][αRibfOPO3H-], is 46 [Lehikoinen89].

Inhibitors (Competitive): formycin A [Bzowska92] , N(6)-methylformycin A [Bzowska92] , formycin B [Bzowska92]

Kinetic Parameters:

Substrate
Km (μM)
Citations
inosine
96.0
[Bennett03a]
phosphate
120.0
[Jensen75]
hypoxanthine
26.6
[Bezirdzhian87]

pH(opt): 7.5 [Jensen75]


Enzymatic reaction of: deoxyinosine phosphorylase (purine nucleoside phosphorylase)

EC Number: 2.4.2.1

2'-deoxyinosine + phosphate <=> hypoxanthine + 2-deoxy-α-D-ribose 1-phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

In Pathways: superpathway of purine deoxyribonucleosides degradation , purine deoxyribonucleosides degradation I

Kinetic Parameters:

Substrate
Km (μM)
Citations
hypoxanthine
26.6
[Bezirdzhian87]
2'-deoxyinosine
106.0
[Bezirdzhian87]

pH(opt): 7.1 [Jensen75]


Enzymatic reaction of: adenosine phosphorylase (purine nucleoside phosphorylase)

EC Number: 2.4.2.1

adenosine + phosphate <=> α-D-ribose-1-phosphate + adenine

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

This reaction is reversible. [Jensen75]

In Pathways: adenine and adenosine salvage III , adenine and adenosine salvage V , purine ribonucleosides degradation

Kinetic Parameters:

Substrate
Km (μM)
Citations
adenine
40.0, 40.0
[Jensen75]
adenosine
46.0
[Bennett03a]
α-D-ribose-1-phosphate
40.0, 40.0
[Jensen75]


Enzymatic reaction of: deoxyadenosine phosphorylase (purine nucleoside phosphorylase)

EC Number: 2.4.2.1

2'-deoxyadenosine + phosphate <=> adenine + 2-deoxy-α-D-ribose 1-phosphate

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

This reaction is reversible.

In Pathways: superpathway of purine deoxyribonucleosides degradation , purine deoxyribonucleosides degradation I

Kinetic Parameters:

Substrate
Km (μM)
Citations
adenine
40.0
[Jensen75]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Henzel93, UniProt11]
UniProt: Removed.
Chain 2 -> 239
[UniProt09]
UniProt: Purine nucleoside phosphorylase deoD- type;
Acetylation-Modification 27
[Zhang09a, UniProt11]
UniProt: N6-acetyllysine.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b4384 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10222; confirmed by SwissProt match.


References

Ahmad68: Ahmad SI, Barth PT, Pritchard RH (1968). "Properties of a mutant of Escherichia coli lacking purine nucleoside phosphorylase." Biochim Biophys Acta 161(2);581-3. PMID: 4875425

Albrechtsen80: Albrechtsen H, Ahmad SI (1980). "Regulation of the synthesis of nucleoside catabolic enzymes in Escherichia coli: further analysis of a deo Oc mutant strain." Mol Gen Genet 1980;179(2);457-60. PMID: 6780756

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

Bennett03a: Bennett EM, Li C, Allan PW, Parker WB, Ealick SE (2003). "Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase." J Biol Chem 278(47);47110-8. PMID: 12937174

Bennett03b: Bennett EM, Anand R, Allan PW, Hassan AE, Hong JS, Levasseur DN, McPherson DT, Parker WB, Secrist JA, Sorscher EJ, Townes TM, Waud WR, Ealick SE (2003). "Designer gene therapy using an Escherichia coli purine nucleoside phosphorylase/prodrug system." Chem Biol 10(12);1173-81. PMID: 14700625

Bertosa14: Bertoša B, Mikleušević G, Wielgus-Kutrowska B, Narczyk M, Hajnic M, Leščić Ašler I, Tomic S, Luic M, Bzowska A (2014). "Homooligomerization is needed for stability: a molecular modelling and solution study of Escherichia coli purine nucleoside phosphorylase." FEBS J 281(7);1860-71. PMID: 24785777

Bezirdzhian86: Bezirdzhian KhO, Kocharian ShM, Akopian ZhI (1986). "[Isolation of the hexameric form of purine nucleoside phosphorylase from E. coli. Comparative study of trimeric and hexameric forms of the enzyme]." Biokhimiia 1986;51(7);1085-92. PMID: 3089333

Bezirdzhian87: Bezirdzhian KhO, Kocharian ShM, Akopian ZhI (1987). "[Hexameric purine nucleoside phosphorylase II from Escherichia coli K-12. Physico-chemical and catalytic properties and stabilization with substrates]." Biokhimiia 1987;52(10);1624-31. PMID: 3122852

Buxton75: Buxton RS (1975). "Genetic analysis of thymidine-resistant and low-thymine-requiring mutants of Escherichia coli K-12 induced by bacteriophage Mu-1." J Bacteriol 121(2);475-84. PMID: 1089630

Bzowska00: Bzowska A, Kulikowska E, Shugar D (2000). "Purine nucleoside phosphorylases: properties, functions, and clinical aspects." Pharmacol Ther 88(3);349-425. PMID: 11337031

Bzowska88: Bzowska A, Kulikowska E, Darzynkiewicz E, Shugar D (1988). "Purine nucleoside phosphorylase. Structure-activity relationships for substrate and inhibitor properties of N-1-, N-7-, and C-8-substituted analogues; differentiation of mammalian and bacterial enzymes with N-1-methylinosine and guanosine." J Biol Chem 263(19);9212-7. PMID: 3132457

Bzowska92: Bzowska A, Kulikowska E, Shugar D (1992). "Formycins A and B and some analogues: selective inhibitors of bacterial (Escherichia coli) purine nucleoside phosphorylase." Biochim Biophys Acta 1120(3);239-47. PMID: 1576149

Dandanell05: Dandanell G, Szczepanowski RH, Kierdaszuk B, Shugar D, Bochtler M (2005). "Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene." J Mol Biol 348(1);113-25. PMID: 15808857

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

Ding10: Ding QB, Ou L, Wei DZ, Wei XK, Xu YM, Zhang CY (2010). "Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli." J Zhejiang Univ Sci B 11(11);880-8. PMID: 21043057

ECOSAL: "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

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

Ge09: Ge C, OuYang L, Ding Q, Ou L (2009). "Co-expression of recombinant nucleoside phosphorylase from Escherichia coli and its application." Appl Biochem Biotechnol 159(1);168-77. PMID: 19099210

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

HammerJespersen71: Hammer-Jespersen K, Munch-Petersen A, Schwartz M, Nygaard P (1971). "Induction of enzymes involed in the catabolism of deoxyribonucleosides and ribonucleosides in Escherichia coli K 12." Eur J Biochem 1971;19(4);533-8. PMID: 4931185

Henzel93: Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C (1993). "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases." Proc Natl Acad Sci U S A 90(11);5011-5. PMID: 8506346

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

Jensen75: Jensen KF, Nygaard P (1975). "Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Purification and some properties." Eur J Biochem 1975;51(1);253-65. PMID: 235429

Jensen76: Jensen KF (1976). "Purine-nucleoside phosphorylase from Salmonella typhimurium and Escherichia coli. Initial velocity kinetics, ligand banding, and reaction mechanism." Eur J Biochem 61(2);377-86. PMID: 813997

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

Koellner02: Koellner G, Bzowska A, Wielgus-Kutrowska B, Luic M, Steiner T, Saenger W, Stepinski J (2002). "Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism." J Mol Biol 315(3);351-71. PMID: 11786017

Koellner98: Koellner G, Luic M, Shugar D, Saenger W, Bzowska A (1998). "Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 A resolution." J Mol Biol 280(1);153-66. PMID: 9653038

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

Lehikoinen89: Lehikoinen PK, Sinnott ML, Krenitsky TA (1989). "Investigation of alpha-deuterium kinetic isotope effects on the purine nucleoside phosphorylase reaction by the equilibrium-perturbation technique." Biochem J 257(2);355-9. PMID: 2494984

Li10c: Li H, Li C (2010). "Multiple ligand simultaneous docking: orchestrated dancing of ligands in binding sites of protein." J Comput Chem 31(10);2014-22. PMID: 20166125

Lomax68: Lomax MS, Greenberg GR (1968). "Characteristics of the deo operon: role in thymine utilization and sensitivity to deoxyribonucleosides." J Bacteriol 96(2);501-14. PMID: 4877128

Mao97a: Mao C, Cook WJ, Zhou M, Koszalka GW, Krenitsky TA, Ealick SE (1997). "The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology." Structure 5(10);1373-83. PMID: 9351810

Mikleuševi11: Mikleušević G, Stefanic Z, Narczyk M, Wielgus-Kutrowska B, Bzowska A, Luic M (2011). "Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies." Biochimie 93(9);1610-22. PMID: 21672603

ModrakWojcik06: Modrak-Wojcik A, Stepniak K, Akoev V, Zolkiewski M, Bzowska A (2006). "Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy." Protein Sci 15(7);1794-800. PMID: 16751611

ModrakWojcik08: Modrak-Wojcik A, Kirilenko A, Shugar D, Kierdaszuk B (2008). "Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP) of bacterial (E. coli) and mammalian (human) origin." Eur Biophys J 37(2);153-64. PMID: 17639373

Parker11: Parker WB, Allan PW, Waud WR, Hong JS, Sorscher EJ (2011). "Effect of expression of adenine phosphoribosyltransferase on the in vivo anti-tumor activity of prodrugs activated by E. coli purine nucleoside phosphorylase." Cancer Gene Ther 18(6);390-8. PMID: 21394111

Pugmire02: Pugmire MJ, Ealick SE (2002). "Structural analyses reveal two distinct families of nucleoside phosphorylases." Biochem J 361(Pt 1);1-25. PMID: 11743878

Rachmeler61: Rachmeler M, Gerhart J, Rosner J (1961). "Limited thymidine uptake in Escherichia coli due to an inducible thymidine phosphorylase." Biochim Biophys Acta 49;222-5. PMID: 13738908

Stein81: Stein RL, Cordes EH (1981). "Kinetic alpha-deuterium isotope effects for Escherichia coli purine nucleoside phosphorylase-catalyzed phosphorolysis of adenosine and inosine." J Biol Chem 256(2);767-72. PMID: 6778874

Svenningsen75: Svenningsen BA (1975). "Regulated in vitro synthesis of the enzymes of the deo operon of Escerichia coli. properties of the DNA directed system." Mol Gen Genet 1975;137(4);289-304. PMID: 810659

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

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

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

ValentinHansen84: Valentin-Hansen P, Hammer K, Love Larsen JE, Svendsen I (1984). "The internal regulated promoter of the deo operon of Escherichia coli K-12." Nucleic Acids Res 1984;12(13);5211-24. PMID: 6087276

Zhang05f: Zhang Y, Parker WB, Sorscher EJ, Ealick SE (2005). "PNP anticancer gene therapy." Curr Top Med Chem 5(13);1259-74. PMID: 16305530

Zhang09a: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

ŠtefaniZ12: Štefanić Z, Narczyk M, Mikleušević G, Wielgus-Kutrowska B, Bzowska A, Luic M (2012). "New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A." FEBS Lett 586(7);967-71. PMID: 22569248

Other References Related to Gene Regulation

Amouyal89: Amouyal M, Mortensen L, Buc H, Hammer K (1989). "Single and double loop formation when deoR repressor binds to its natural operator sites." Cell 1989;58(3);545-51. PMID: 2667765

Brikun96: Brikun I, Suziedelis K, Stemmann O, Zhong R, Alikhanian L, Linkova E, Mironov A, Berg DE (1996). "Analysis of CRP-CytR interactions at the Escherichia coli udp promoter." J Bacteriol 1996;178(6);1614-22. PMID: 8626289

Chahla03: Chahla M, Wooll J, Laue TM, Nguyen N, Senear DF (2003). "Role of protein-protein bridging interactions on cooperative assembly of DNA-bound CRP-CytR-CRP complex and regulation of the Escherichia coli CytR regulon." Biochemistry 42(13);3812-25. PMID: 12667072

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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