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Literature summary for 3.2.2.3 extracted from

  • Kopecna, M.; Blaschke, H.; Kopecny, D.; Vigouroux, A.; Koncitikova, R.; Novak, O.; Kotland, O.; Strnad, M.; Morera, S.; von Schwartzenberg, K.
    Structure and function of nucleoside hydrolases from Physcomitrella patens and maize catalyzing the hydrolysis of purine, pyrimidine, and cytokinin ribosides (2013), Plant Physiol., 163, 1568-1583.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.2.3

Cloned(Commentary)

Cloned (Comment) Organism
isozyme PpNRH2, phylogenetic analysis, recombinant expression in Escherichia coli in inclusion bodies Physcomitrium patens
phylogenetic analysis Zea mays

Protein Variants

Protein Variants Comment Organism
additional information functional knockout of the mutant, phenotypic analysis of wild-type and mutant enzymes, overview Physcomitrium patens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information substrate specificity and kinetics, overview Zea mays
0.06
-
 adenosine pH 7.5, 30°C, recombinant enzyme Zea mays
0.109
-
 Xanthosine pH 7.5, 30°C, recombinant enzyme Zea mays
0.111
-
 adenosine pH 7.5, 30°C, recombinant enzyme Zea mays
0.178
-
 Xanthosine pH 7.5, 30°C, recombinant enzyme Zea mays
0.468
-
 uridine pH 7.5, 30°C, recombinant enzyme Zea mays
0.512
-
 uridine pH 7.5, 30°C, recombinant enzyme Zea mays
0.713
-
 Inosine pH 7.5, 30°C, recombinant enzyme Zea mays
1.013
-
 Inosine pH 7.5, 30°C, recombinant enzyme Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
uridine + H2O Zea mays
-
 D-ribose + uracil
-
 ?
uridine + H2O Physcomitrium patens
-
 D-ribose + uracil
-
 ?

Organism

Organism UniProt Comment Textmining
Physcomitrium patens
-
-
-
Zea mays
-
-
-
Zea mays H9D3U7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine + H2O 15% of the activity with uridine Zea mays D-ribose + adenine
-
 ?
adenosine + H2O 3.5% of the activity with uridine Zea mays D-ribose + adenine
-
 ?
cytidine + H2O 3.9% of the activity with uridine Physcomitrium patens D-ribose + cytosine
-
 ?
cytidine + H2O 5.0% of the activity with uridine Zea mays D-ribose + cytosine
-
 ?
inosine + H2O 22% of the activity with uridine Physcomitrium patens D-ribose + hypoxanthine
-
 ?
inosine + H2O 9.3% of the activity with uridine Zea mays D-ribose + hypoxanthine
-
 ?
inosine + H2O 9.5% of the activity with uridine Zea mays D-ribose + hypoxanthine
-
 ?
additional information adenosine is a poor substrates, no activity with guanosine, trans-zeatin riboside, and cytokinin riboside, substrate specificity, overview Physcomitrium patens ?
-
 ?
additional information no or almost no activity with guanosine, trans-zeatin riboside, and cytokinin riboside, substrate specificity, overview Zea mays ?
-
 ?
additional information poor activity with cytidine, guanosine, trans-zeatin riboside, and cytokinin riboside, substrate specificity, overview Zea mays ?
-
 ?
uridine + H2O
-
 Zea mays D-ribose + uracil
-
 ?
uridine + H2O
-
 Physcomitrium patens D-ribose + uracil
-
 ?
uridine + H2O best substrate Zea mays D-ribose + uracil
-
 ?
uridine + H2O best substrate Physcomitrium patens D-ribose + uracil
-
 ?
xanthosine + H2O 34% of the activity with uridine Zea mays D-ribose + xanthine
-
 ?
xanthosine + H2O 53% of the activity with uridine Zea mays D-ribose + xanthine
-
 ?
xanthosine + H2O 61% of the activity with uridine Physcomitrium patens D-ribose + xanthine
-
 ?

Synonyms

Synonyms Comment Organism
PpNRH2
-
 Physcomitrium patens
ZmNRH2a
-
 Zea mays
ZmNRH2b
-
 Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Zea mays
30
-
 assay at Physcomitrium patens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.18
-
 adenosine pH 7.5, 30°C, recombinant enzyme Zea mays
0.4
-
 adenosine pH 7.5, 30°C, recombinant enzyme Zea mays
0.61
-
 Inosine pH 7.5, 30°C, recombinant enzyme Zea mays
1.3
-
 Xanthosine pH 7.5, 30°C, recombinant enzyme Zea mays
3
-
 uridine pH 7.5, 30°C, recombinant enzyme Zea mays
4.1
-
 Inosine pH 7.5, 30°C, recombinant enzyme Zea mays
4.6
-
 Xanthosine pH 7.5, 30°C, recombinant enzyme Zea mays
23.8
-
 uridine pH 7.5, 30°C, recombinant enzyme Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Zea mays
7.5
-
 assay at Physcomitrium patens

General Information

General Information Comment Organism
malfunction changes in the levels of purine, pyrimidine, and cytokinin metabolites in knockout mutants, phenotypes, overview Physcomitrium patens
additional information the presence of a tyrosine at position 249 (PpNRH1 numbering) confers high hydrolase activity for purine ribosides Zea mays
additional information the presence of a tyrosine at position 249 (PpNRH1 numbering) confers high hydrolase activity for purine ribosides Physcomitrium patens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.6
-
 Inosine pH 7.5, 30°C, recombinant enzyme Zea mays
3
-
 adenosine pH 7.5, 30°C, recombinant enzyme Zea mays
3.5
-
 adenosine pH 7.5, 30°C, recombinant enzyme Zea mays
5.7
-
 Inosine pH 7.5, 30°C, recombinant enzyme Zea mays
6.4
-
 uridine pH 7.5, 30°C, recombinant enzyme Zea mays
7.5
-
 Xanthosine pH 7.5, 30°C, recombinant enzyme Zea mays
42
-
 Xanthosine pH 7.5, 30°C, recombinant enzyme Zea mays
46
-
 uridine pH 7.5, 30°C, recombinant enzyme Zea mays