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Information on EC 4.6.1.24 - ribonuclease T1 and Organism(s) Kitasatospora aureofaciens and UniProt Accession P05798

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Kitasatospora aureofaciens
UNIPROT: P05798 not found.
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The taxonomic range for the selected organisms is: Kitasatospora aureofaciens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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[RNA] containing guanosine
+
H2O
=
an [RNA fragment]-3'-guanosine-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
[RNA] containing guanosine
+
=
an [RNA fragment]-3'-guanosine-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
Synonyms
rnase a, ribonuclease a, barnase, rnase t1, ribonuclease t1, binase, rnase g, rnase sa, rnase ms, ribonuclease sa, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanylate endoribonuclease
-
Aspergillus oryzae ribonuclease
-
-
-
-
Binase
-
-
-
-
Guanyl-specific RNase
-
-
-
-
Guanyloribonuclease
-
-
-
-
Nuclease, guanyloribo-
-
-
-
-
Nuclease, ribo-, Aspergillus oryzae
-
-
-
-
Ribonuclease C2
-
-
-
-
Ribonuclease Ch
-
-
-
-
Ribonuclease F1
-
-
-
-
Ribonuclease guaninenucleotido-2'-transferase (cyclizing)
-
-
-
-
Ribonuclease N1
-
-
-
-
Ribonuclease N3
-
-
-
-
Ribonuclease PP1
-
-
-
-
Ribonuclease SA
ribonuclease Sa2
-
-
Ribonuclease U1
-
-
-
-
RNase F1
-
-
-
-
RNase Fl1
-
-
-
-
RNase Fl2
-
-
-
-
RNase G
-
-
-
-
RNase Ms
-
-
-
-
RNase N1
-
-
-
-
RNase N2
-
-
-
-
RNase Pb1
-
-
-
-
RNase Pc
-
-
-
-
RNase Po1
-
-
-
-
RNase Sa
RNase Sa3
-
-
-
-
RNase St
-
-
-
-
RNase T1
-
-
-
-
RNase Th1
-
-
-
-
RNase U1
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
show the reaction diagram
hydrolysis of the phosphodiester bonds of single-stranded RNA at the 3'-side of guanosine nucleotides occurs with high specificity
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-12-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3'-N-hydroxyurea-3'-deoxythymidine-5'-phosphate
competitive, inhibition is enhanced by nearly 10fold in presence of Zn2 in wild-type enzyme, no enhancement in mutant enzyme E54Q
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.151 - 0.4
poly(I)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 460
poly(I)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.95 - 1.15
3'-N-hydroxyurea-3'-deoxythymidine-5'-phosphate
0.000033
chitosan
-
poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RNSA_KITAU
96
0
10576
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion
mutant enzyme Q94K, hanging-drop vapor-diffusion method at 18°C
RNase Sa-3'IMP complex
structures of two crystal forms (I and II) of ribonuclease Sa2 are presented at 1.8 A and 1.5 A resolution. Vapour diffusion from a solution of 1.0% protein by weight in 0.1 M phosphate buffer at pH 7.2 and room temperature with 40% saturated ammonium sulfate as precipitant
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D33A
Tm-value at pH 7.0 in Mops buffer is 16 °C lower than wild-type value. The stability of the mutant enzyme is 6 kcal/mol less than wild-type RNase Sa
D79A
Tm-value at pH 7.0 in Mops buffer is 9.2 °C higher than wild-type value. The stability of the mutant enzyme is 3.3 kcal/mol less than wild-type RNase Sa
D79E
Tm-value at pH 7.0 in Mops buffer is 0.8 °C lower than wild-type value. kcat/Km is identical to wild-type value
D79F
Tm-value at pH 7.0 in Mops buffer is 9.9 °C higher than wild-type value
D79H
Tm-value at pH 7.0 in Mops buffer is 5.6 °C higher than wild-type value
D79I
Tm-value at pH 7.0 in Mops buffer is 9.6 °C higher than wild-type value. kcat/Km is 1.3fold lower than wild-type value
D79K
Tm-value at pH 7.0 in Mops buffer is 7.6 °C higher than wild-type value. kcat/Km is 1.1fold lower than wild-type value
D79L
Tm-value at pH 7.0 in Mops buffer is 8.7 °C higher than wild-type value
D79N
Tm-value at pH 7.0 in Mops buffer is 5.5 °C higher than wild-type value. kcat/Km is 1.1fold lower than wild-type value
D79R
Tm-value at pH 7.0 in Mops buffer is 9.0 °C higher than wild-type value. kcat/Km is 1.1fold higher than wild-type value
D79W
Tm-value at pH 7.0 in Mops buffer is 7.6 °C higher than wild-type value. kcat/Km is 1.2fold lower than wild-type value
D79Y
Tm-value at pH 7.0 in Mops buffer is 9.6 °C higher than wild-type value
Q94K
Tm-value at pH 7.0 in Mops buffer is 0.8 °C higher than wild-type value. Crystal structure shows that the amino group of the Lys forms a hydrogen-bonded ion pair with the carboxyl group of Asp79. The stability of the mutant is about the same as the wild-type at pH 3, where Asp79 is uncharged, but 1 kcal/mol greater than that of wild-type RNase Sa at pH 8.5, where Asp79 is charged
D1W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
T76W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
Y52W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
Y55W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
Y81W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NaCl and low concentrations of guanidinium chloride stabilize RNase Sa, conformational stability is studied by NMR-monitored hydrogen exchange
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion-exchange chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
RNase inhibitors appear to be promising for therapy of cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sevcik, J.; Lamzin, V.S.; Dauter, Z.; Wilson, K.S.
Atomic resolution data reveal flexibility in the structure of RNase Sa
Acta Crystallogr. Sect. D
58
1307-1313
2002
Kitasatospora aureofaciens (P05798), Kitasatospora aureofaciens
Manually annotated by BRENDA team
Sevcik, J.; Dauter, Z.; Wilson, K.S.
Crystal structure reveals two alternative conformations in the active site of ribonuclease Sa2
Acta Crystallogr. Sect. D
D60
1198-1204
2004
Kitasatospora aureofaciens
Manually annotated by BRENDA team
Makarov, A.A.; Yakovlev, G.I.; Mitkevich, V.A.; Higgin, J.J.; Raines, R.T.
Zinc(II)-mediated inhibition of ribonuclease Sa by an N-hydroxyurea nucleotide and its basis
Biochem. Biophys. Res. Commun.
319
152-156
2004
Kitasatospora aureofaciens (P05798), Kitasatospora aureofaciens
Manually annotated by BRENDA team
Laurents, D.V.; Scholtz, J.M.; Rico, M.; Pace, C.N.; Bruix, M.
Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange
Biochemistry
44
7644-7655
2005
Kitasatospora aureofaciens (P05798)
Manually annotated by BRENDA team
Trevino, S.R.; Gokulan, K.; Newsom, S.; Thurlkill, R.L.; Shaw, K.L.; Mitkevich, V.A.; Makarov, A.A.; Sacchettini, J.C.; Scholtz, J.M.; Pace, C.N.
Asp79 makes a large, unfavorable contribution to the stability of RNase Sa
J. Mol. Biol.
354
967-978
2005
Kitasatospora aureofaciens (P05798)
Manually annotated by BRENDA team
Schrift, G.L.; Waldron, T.T.; Timmons, M.A.; Ramaswamy, S.; Kearney, W.R.; Murphy, K.P.
Molecular basis for nucleotide-binding specificity: role of the exocyclic amino group "N2" in recognition by a guanylyl-ribonuclease
J. Mol. Biol.
355
72-84
2006
Kitasatospora aureofaciens (P05798), Kitasatospora aureofaciens
Manually annotated by BRENDA team
Yakovlev, G.I.; Mitkevich, V.A.; Struminskaya, N.K.; Varlamov, V.P.; Makarov, A.A.
Low molecular weight chitosan is an efficient inhibitor of ribonucleases
Biochem. Biophys. Res. Commun.
357
584-588
2007
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus intermedius, Bos taurus, Penicillium brevicompactum, Kitasatospora aureofaciens
Manually annotated by BRENDA team
Alston, R.W.; Lasagna, M.; Grimsley, G.R.; Scholtz, J.M.; Reinhart, G.D.; Pace, C.N.
Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa
Biophys. J.
94
2288-2296
2008
Kitasatospora aureofaciens
Manually annotated by BRENDA team