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Information on EC 2.4.2.1 - purine-nucleoside phosphorylase and Organism(s) Bacillus subtilis and UniProt Accession P46354

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.1 purine-nucleoside phosphorylase
IUBMB Comments
Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P46354
Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
5'-deoxy-5'-methylthioadenosine phosphorylase II, 5'-methythioadenosine phosphorylase, adenine nucleoside phosphorylase, adenosine phosphorylase, AgPNP, ANP, ApMTAP, apPNP, bovPNP, bPNO, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine phosphorylase
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DeoD
298591
gene name
inosine phosphorylase
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inosine-guanosine phosphorylase
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nucleotide phosphatase (2.4.2.1)
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phosphorylase, purine nucleoside
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PNPase
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Pu-NPase
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PUNP
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PUNPI
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PUNPII
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purine deoxynucleoside phosphorylase
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purine deoxyribonucleoside phosphorylase
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purine nucleoside phosphorylase
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purine ribonucleoside phosphorylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
purine-nucleoside:phosphate ribosyltransferase
Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-21-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine + phosphate
adenine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
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isoform of 816 amino acids, 1% of the activity with inosine, isoform of 702 amino acids, 15% of the activity with inosine
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-
?
2'-deoxyguanosine + phosphate
guanine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
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isoform of 816 amino acids, 17% of the activity with inosine, isoform of 702 amino acids, 18% of the activity with inosine
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-
?
2'-deoxyinosine + phosphate
hypoxanthine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
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isoform of 816 amino acids, 23% of the activity with inosine, isoform of 702 amino acids, 31% of the activity with inosine
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-
?
adenosine + phosphate
adenine + alpha-D-ribose 1-phosphate
show the reaction diagram
deoxyadenosine + phosphate
alpha-D-ribose 1-phosphate + adenine
show the reaction diagram
deoxyguanosine + phosphate
guanine + alpha-D-deoxyribose 1-phosphate
show the reaction diagram
deoxyinosine + phosphate
hypoxanthine + alpha-D-deoxyribose 1-phosphate
show the reaction diagram
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
show the reaction diagram
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
additional information
?
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two purine nucleoside phosphorylases: 1. inosine-guanosine phosphorylase, 2. adenosine-specific phosphorylase
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
guanosine
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strong competitive inhibitor with deoxyinosine as substrate
Inosine
PCMB
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adenosine-specific phosphorylase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00031 - 0.2
Inosine
3.9
phosphate
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reaction with inosine, inosine-guanosine phosphorylase
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3900 - 12000
Inosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
320000 - 3900000
Inosine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73
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adenosine-specific phosphorylase
100
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inosine-guanosine phosphorylase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25500
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6 * 25500, adenosine-specific phosphorylase, SDS-PAGE
28000
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x * 28000, inosine-guanosine phosphorylase, SDS-PAGE
95000
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inosine-guanosine phosphoylase, gel filtration
153000
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adenosine-specific phosphorylase, gel filtration
164200
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 28000, inosine-guanosine phosphorylase, SDS-PAGE
hexamer
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
Crystals belonging to space groups P321, P212121, P6322 and H32 are grown in distinct conditions with pH values ranging from 4.2 to 10.5. The crystals diffracts to maximum resolutions ranging from 2.65 to 1.70 A
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
two purine nucleoside phosphorylases: 1. inosine-guanosine phosphorylase, 2. adenosine-specific phosphorylase
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Parks, R.E.; Agarwal, R.P.
Purine nucleoside phosphorylase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
483-514
1972
Aeromonas hydrophila, Bacillus cereus, Bacillus licheniformis, Bacillus subtilis, Bacterium cadaveris, Bos taurus, Brevibacillus brevis, Canis lupus familiaris, Clavibacter michiganensis subsp. sepedonicus, Columba livia, Equus caballus, Escherichia coli, Felis catus, Gallus gallus, Homo sapiens, Klebsiella aerogenes, Lactobacillus leichmannii, Leucisus rusticus, Macaca mulatta, Micrococcus luteus, Oryctolagus cuniculus, Papio hamadryas, Pectobacterium carotovorum, Proteus vulgaris, Rattus norvegicus, salmon, Salmonella enterica subsp. enterica serovar Enteritidis, Shewanella putrefaciens, Sus scrofa
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Manually annotated by BRENDA team
Jensen, K.J.
Two purine nucleoside phosphorylases in Bacillus subtilis. Purification and some properties of the adenosine-specific phosphorylase
Biochim. Biophys. Acta
525
346-356
1978
Bacillus subtilis
Manually annotated by BRENDA team
Bzowska, A.; Kulikowska, E.; Shugar, D.
Purine nucleoside phosphorylases: properties, functions, and clinical aspects
Pharmacol. Ther.
88
349-425
2000
Acholeplasma laidlawii, Bacillus cereus, Bacillus subtilis (P46354), Bos taurus (P55859), Cellulomonas sp., Escherichia coli (P0ABP8), Fasciola hepatica, Geobacillus stearothermophilus, Homo sapiens, Homo sapiens (P00491), Klebsiella aerogenes, Klebsiella sp., Micrococcus luteus, Mus musculus, Pectobacterium carotovorum, Plasmodium falciparum, Plasmodium lophurae, Proteus vulgaris, Rattus norvegicus, Saccharolobus solfataricus, Saccharomyces cerevisiae (Q05788), Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Trypanosoma brucei, Trypanosoma cruzi
Manually annotated by BRENDA team
Martins, N.H.; Meza, A.N.; Santos, C.R.; de Giuseppe, P.O.; Murakami, M.T.
Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of a purine nucleoside phosphorylase from Bacillus subtilis strain 168
Acta Crystallogr. Sect. F
67
618-622
2011
Bacillus subtilis 168 (O34925), Bacillus subtilis, Bacillus subtilis (O34925)
Manually annotated by BRENDA team
Xie, X.; Xia, J.; He, K.; Lu, L.; Xu, Q.; Chen, N.
Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs
Biotechnol. Lett.
33
1107-1112
2011
Bacillus subtilis 168, Bacillus subtilis, Escherichia coli, Pseudoalteromonas sp.
Manually annotated by BRENDA team
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