Information on EC 6.5.1.4 - RNA 3'-terminal-phosphate cyclase (ATP)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
6.5.1.4
-
RECOMMENDED NAME
GeneOntology No.
RNA 3'-terminal-phosphate cyclase (ATP)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
formation of a covalent cyclase-AMP intermediate
-
ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
upon binding of Mg2+ to residue E10, the triphosphate group of the trapped ATP changes its conformation, with help of ligands R17 and R39. The Nepsilon atom of H307 attacks the alpha-phosphate group to form a new P-N bond. When a truncated RNA is bound, its 3'-phosphate group may be forced to react with the phosphate group of AMP, and the activated 3'-phosphate group may be attacked by the 2'-hydroxyl group to generate the 2',3'-cyclic phosphodiester
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cyclization
-
-
esterification
-
-
cyclic phosphomonoester
-
Ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
RNA-3'-phosphate:RNA ligase (cyclizing, AMP-forming)
Adenosine 5'-(gamma-thio)triphosphate can act instead of ATP. cf. EC 6.5.1.5, RNA-3'-phosphate cyclase (GTP).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
RNA 3'-phosphate cyclase
-
-
RNA 3'-phosphate cyclase
-
-
RNA 3'-phosphate cyclase
-
-
RNA 3'-teminal phosphate cyclase
-
-
RNA 3'-terminal phosphate cyclase
-
-
-
-
RNA 3'-terminal phosphate cyclase
P46849
-
RNA 3'-terminal phosphate cyclase
Escherichia coli K12
-
-
-
RNA 3'-terminal phosphate cyclase
-
-
RNA 3'-terminal phosphate cyclase
-
-
RNA 3'-terminal phosphate cylase
-
-
RNA cyclase
-
-
-
-
RNA-3'-phosphate cyclase
-
-
-
-
Rtc1
-
-
RtcA
P46849
-
CAS REGISTRY NUMBER
COMMENTARY
85638-41-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
zebra fish
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
strain YMC10
Uniprot
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
Escherichia coli YMC10
strain YMC10
Uniprot
Manually annotated by BRENDA team
no activity in Bacillus subtilis
-
-
-
Manually annotated by BRENDA team
no activity in Haemophilus influenzae
-
-
-
Manually annotated by BRENDA team
no activity in Helicobacter pylori
-
-
-
Manually annotated by BRENDA team
no activity in Mycoplasma genitalium
-
-
-
Manually annotated by BRENDA team
no activity in Synechocystis sp.
-
-
-
Manually annotated by BRENDA team
fission yeast
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
synthesis of RNA 2',3' cyclic phosphate ends via an ATP-dependent pathway comprising three nucleotidyl transfer steps: reaction of Rtc with ATP to form a covalent Rtc-(histidinyl-N)-AMP intermediate and release PPi, transfer of AMP from Rtc1 to an RNA 3'-phosphate to form an RNA(3')pp(5')A intermediate; and attack by the terminal nucleoside O2' on the 3'-phosphate to form an RNA 2',3' cyclic phosphate product and release AMP
metabolism
-
synthesis of RNA 2',3'-cyclic phosphate ends via an ATP-dependent pathway comprising three nucleotidyl transfer steps: reaction of Rtc with ATP to form a covalent Rtc-(histidinyl-N)-AMP intermediate and release diphosphate, transfer of AMP from Rtc1 to an RNA 3'-phosphate to form an RNA(3')pp(5')A intermediate; and attack by the terminal nucleoside O2' on the 3'-phosphate to form an RNA 2',3'-cyclic phosphate product and release AMP
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (Ap)npAp
AMP + ?
show the reaction diagram
-
pure oligoribonucleotide
-
?
ATP + (Up)10pGp
AMP + ?
show the reaction diagram
-
pure oligoribonucleotide
-
?
ATP + 5S rRNA
AMP + ?
show the reaction diagram
-, P46850
-
-
?
ATP + 5S rRNA
AMP + ?
show the reaction diagram
-
modified by ligation of [5'-P]pCp to the 3'-terminus
-
?
ATP + 5S rRNA-pCp
AMP + ?
show the reaction diagram
-
-
-
?
ATP + AAAACAAAAGp
AMP + ?
show the reaction diagram
P46849
-
-
?
ATP + AAAAUAAAAGCp
AMP + ?
show the reaction diagram
-
pure oligoribonucleotide
-
?
ATP + AAAAUAAAAGp
AMP + ?
show the reaction diagram
Escherichia coli, Homo sapiens, Escherichia coli K12
-
pure oligoribonucleotide
-
?
ATP + AAAAUAAAAGpCp
AMP + diphosphate + AAAAUAAAAGpC-2',3'-cyclic phosphate
show the reaction diagram
-
-
-
-
ir
ATP + AAAAUAAAAGpCp
AMP + diphosphate + AAAAUAAAAGpC-2',3'-cyclic phosphate
show the reaction diagram
-
-
-
-
ir
ATP + AUGp
AMP + ?
show the reaction diagram
-
pure oligoribonucleotide
-
?
ATP + CCCCACCCCGp
AMP + ?
show the reaction diagram
Escherichia coli, Homo sapiens, Escherichia coli K12
-
pure oligoribonucleotide
-
?
ATP + CCCCCACCCCGCp
AMP + ?
show the reaction diagram
-
pure oligoribonucleotide
-
?
ATP + DNA 5'-terminal-phosphate
AMP + AppDNA
show the reaction diagram
-
RtcA also catalyzes adenylylation of 5'-phosphate ends of DNA strands to form AppDNA product
-
-
?
ATP + human U14 snoRNA
AMP + ?
show the reaction diagram
-, P46850
-
-
?
ATP + human U14 snoRNA
AMP + ?
show the reaction diagram
-
modified by ligation of [5'-P]pCp to the 3'-terminus
-
?
ATP + oligodeoxyribonucleotide 3'-terminal phosphate
AMP + diphosphate + oligodeoxyribonucleotide-2',3'-cyclic-phosphate
show the reaction diagram
-, O00442
500fold poorer substrate than oligoribonucleotide 3'-terminal phosphate
-
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
no activity with dATP
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
ir, (Up)10Gp is cyclized at a faster rate than tRNAApGp or AUGp
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
human U6 small nuclear RNA
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-, O00442
oligoribonucleotides
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphodiester
show the reaction diagram
-
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphodiester
show the reaction diagram
-, P46850
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphodiester
show the reaction diagram
-
-
-
?
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphodiester
show the reaction diagram
P46849
-
-
?
ATP + RNA 3'-terminal-phosphate
?
show the reaction diagram
-, O00442
the enzyme could be involved in the maintenance of cyclic ends in tRNA splicing intermediates or in the cyclization of the 3' end of U6 sbRNA
-
-
-
ATP + RNA 3'-terminal-phosphate
?
show the reaction diagram
-
role in RNA processing
-
-
-
ATP + RNA 3'-terminal-phosphate
AMP + diphosphate + RNA terminal-2',3'-cyclic phosphate
show the reaction diagram
-
RtcA catalyzes the synthesis of RNA 2',3'-cyclic phosphate ends via an ATP-dependent pathway comprising three nucleotidyl transfer steps: reaction of RtcA with ATP to form a covalent RtcA-(histidinyl-N)-AMP intermediate and release diphosphate, transfer of AMP from RtcA to an RNA 3'-phosphate to form an RNA(3')pp(5')A intermediate, and attack by the terminal nucleoside O2' on the 3'-phosphate to form an RNA 2',3'-cyclic phosphate product and release AMP
-
-
?
ATP + RNA 5'-terminal-phosphate
AMP + AppRNA
show the reaction diagram
-
RtcA also catalyzes adenylylation of 5'-phosphate ends of RNA strands to form AppRNA product
-
-
?
ATP + tobacco mosaic virus RNA
AMP + ?
show the reaction diagram
-
fragments modified by ligation of pGp, pAp, or pCp
-
?
ATP + tRNA-pNp
AMP + ?
show the reaction diagram
-
-
-
?
ATPgammaS + RNA 3'-terminal-phosphate
AMP + thiodiphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
-
ATPgammaS + RNA 3'-terminal-phosphate
AMP + thiodiphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
ir
-
-
CTP + RNA 3'-terminal-phosphate
CMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
-
CTP + RNA 3'-terminal-phosphate
CMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
reaction proceeds 15-20 times slower than in presence of ATP
-
-
-
GTP + RNA 3'-terminal-phosphate
GMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
-
GTP + RNA 3'-terminal-phosphate
GMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
-
GTP + RNA 3'-terminal-phosphate
GMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
reaction proceeds 15-20 times slower than in presence of ATP
-
-
-
RNA-N3'p + ATP
RNA-N-2',3'-cyclic phosphate + AMP + diphosphate
show the reaction diagram
-
-
-
-
ir
UTP + RNA 3'-terminal-phosphate
UMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
-
-
-
-
UTP + RNA 3'-terminal-phosphate
UMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
-
reaction proceeds 15-20 times slower than in presence of ATP
-
-
-
GTP + RNA 3'-terminal-phosphate
GMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
additional information
?
-
-
ATP/diphosphate exchange reaction not detected
-
-
-
additional information
?
-
-
nucleoside 3'-monophosphates and nucleoside 5',3'-bisphosphates are no substrates
-
?
additional information
?
-
-
trinucleotides are the shortest oligonucleotides able to act as substrates, ribonucleoside 3'-phosphates and ribonucleoside 5',3'-phosphates are no substrates
-
?
additional information
?
-
-
it was suggested that the enzyme could be responsible for the generation of the 2',3'-cyclic termini required for ligation of RNA by eukaryotic ligases and, consequently, be involved in tRNA slicing. It was found, however, that the slicing endonucleases responsible for the excision of introns from tRNA precursors in yeast and Xenopus sp. directly produce RNA molecules with cyclic phosphate ends
-
-
-
additional information
?
-
-, P46850
nonessential as demonstrated by knockout experiments
-
?
additional information
?
-
P46849
precise function is not known, may be responsible for generating or regenerating cyclic phosphate RNA ends required by RNA ligases
-
?
additional information
?
-
-
RtcA readily adenylylates the 5'-phosphate at a 5'-PO4/3'-OH nick in duplex DNA but is unable to covert the nicked DNA-adenylate to a sealed phosphodiester
-
-
-
additional information
?
-
-
RtcB per se seals broken tRNA-like stem-loop structures with 2',3'-cyclic phosphate and 5'-OH ends to form a splice junction with a 2'-OH, 3',5'-phosphodiester
-
-
-
additional information
?
-
Escherichia coli K12
-
nucleoside 3'-monophosphates and nucleoside 5',3'-bisphosphates are no substrates
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + RNA 3'-terminal-phosphate
?
show the reaction diagram
-, O00442
the enzyme could be involved in the maintenance of cyclic ends in tRNA splicing intermediates or in the cyclization of the 3' end of U6 sbRNA
-
-
-
ATP + RNA 3'-terminal-phosphate
?
show the reaction diagram
-
role in RNA processing
-
-
-
additional information
?
-
-
it was suggested that the enzyme could be responsible for the generation of the 2',3'-cyclic termini required for ligation of RNA by eukaryotic ligases and, consequently, be involved in tRNA slicing. It was found, however, that the slicing endonucleases responsible for the excision of introns from tRNA precursors in yeast and Xenopus sp. directly produce RNA molecules with cyclic phosphate ends
-
-
-
additional information
?
-
-, P46850
nonessential as demonstrated by knockout experiments
-
?
additional information
?
-
P46849
precise function is not known, may be responsible for generating or regenerating cyclic phosphate RNA ends required by RNA ligases
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
requires ATP as cofactor, other ribonucleoside triphosphates are used very inefficiently
ATP
-
ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
only 5% of the activation by Mg2+
K+
-
optimal concentration: 150-200 mM
Mg2+
-
Km: 2.5 mM; required
Mg2+
-
maximal activity at 4-5 mM; required
Mg2+
-
maximal activity at 4-5 mM
Mg2+
-
required for activity, 2 mM Mg2+ is used in assay conditions
Mn2+
-
cannot replace Mg2+ in activation
Mn2+
-
only 5% of the activation by Mg2+
Mn2+
-
able to replace Mg2+
Na+
-
optimal concentration: 150-200 mM
Mn2+
-, P46850
-
additional information
-
no activity with Ca2+, Zn2+, or Cu2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
-
-
pC3'p
-, P46850
-
pdCp
-, P46850
-
Sodium phosphate
-
-
Vanadyl-ribonucleoside complex
-
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0017
-
ATP
-
-
0.002
-
ATP
-
-
0.006
-
ATP
-
-
0.02
-
ATP
-, P46850
pH 7.6, 25C
0.006
-
ATPgammaS
-
-
0.006
-
ATPgammaS
-
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.021
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
6
-
pH-optimum for DNA 5'-adenylylation Tris acetate buffer
8
8.5
-
pH-optimum for RNA 3'-cyclization
8.5
-
-, P46850
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10
-, P46850
-
8
10.5
-
8.0-9.0: maximal activity, 10.5: 70% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
similar rates of reaction at 25C, 30C, and 37C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
37
-
0C: 25% of maximal activity, 12C: 60% of maximal activity, 25-37C: maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
38000
40000
-
glycerol density gradient sedimentation, gel filtration
39000
-
-
SDS-PAGE
39400
-
-
calculated from cDNA
40000
-
-
SDS-PAGE
40000
-
-
predicted from open reading frame
40000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homodimer
-
the apoenzyme of Escherichia coli RtcA crystallizes as a disulfide-linked homodimer and reveales a fold composed of four tandem modules, each comprising a four-stranded beta sheet overlying two alpha helices, X-ray diffraction
monomer
-
1 * 38000-40000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion technique, 2 orthorhombic crystal forms, space group P2(1)2(1)2(1), unit-cell dimensions a : 101.8 A, b : 126.6 A and c : 128.8 A, and P2(1)2(1)2 with unit cell dimensions a : 125.8 A, b : 133.5 A, c : 51.0 A
-
crystallized in the states St-Rtc, St-Rtc+Mn, St-Rtc+ATP, St-Rtc+AMP and St-Rtc-AMP
-
native enzyme, with AMP covalently bound, in complex with AMP, with ATP, or Mn2+, at 2.25 A, 2.25A, 2.9 A, 2.4 A and 3.2 A resolutions, respectively. Upon binding of Mg2+ to residue E10, the triphosphate group of the trapped ATP changes its conformation, with help of ligands R17 and R39. The Nepsilon atom of H307 attacks the alpha-phosphate group to form a new P-N bond. When a truncated RNA is bound, its 3'-phosphate group may be forced to react with the phosphate group of AMP, and the activiated 3'-phosphate group may be attacked by the 2'-hydroxyl group to generate the 2',3'-cyclic phosphodiester
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
3 d, 50% loss of activity
20
-
-
3-4 h, 50% loss of activity
42
-
-
5 min, 55% loss of activity
50
-
-
5 min, 95% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
not affected by several cycles of freezing and thawing
-
resistant to protease digestion
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, stable for at least 3 months
-
-70C, stable for at least 6 months
-
4C, 50% loss of activity after 3 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene encoding cyclase like protein present
-
expressed sequence tags encoding cyclase like protein identified
-
bacterially overexpressed as a fusion protein
-
cloned and overexpressed
-
expressed in Escherichia coli BL21-Codon Plus (DE3)
-
gene rtcA cloned and overexpressed
-, P46850
gene rtcA encoding cyclase cloned and overexpressed
-
cDNA characterized
-
cloned and overexpressed in Escherichia coli as fusion protein with glutathione S-transferase
-
expressed in Escherichia coli
-
overexpression in Escherichia coli
-, O00442
gene encoding cyclase like protein present
-
cDNA characterized, complements yeast strains depleted of Rcl1p
-
expressed sequence tags encoding cyclase like protein identified
-
gene encoding cyclase like protein present
-
expressed sequence tags encoding cyclase like protein identified
-
expressed sequence tags encoding cyclase like protein identified
-
expression in Escherichia coli
-
overexpressed in Escherichia coli
-
expressed sequence tags encoding cyclase like protein identified
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C308A
-
recombinant mutant protein
D287A
-
activity very low, 1% of wild-type enzyme
E270A
-
reduced activity compared to wild-type enzyme, about 80%
F135A
-
activity very low, 3% of wild-type enzyme
F251A
-
considerably reduced activity compared to wild-type enzyme, about 30%
H309A
-
activity very low, less than 10% of wild-type enzyme
H309G
-
enzyme inactive
P131G
-
considerably reduced activity compared to wild-type enzyme, about 35%
Q104A
-
almost same activiy like wild-type enzyme
Q288A
-
activity very low, 2% of wild-type enzyme
S129A
-
almost same activiy like wild-type enzyme
Y284A
-
considerably reduced activity compared to wild-type enzyme (12%)
D297A
-
enzyme inactive
E14A
-
activity very low, only 4% of RNA is cyclized compared to 95% with wild-type enzyme
H320A
-
enzyme inactive
H326A
-
almost same activiy like wild-type enzyme
H52A
-
half activity compared to wild-type enzyme
Q51A
-
almost same activiy like wild-type enzyme
R21A
-
enzyme inactive
R40A
-
enzyme inactive
R43A
-
enzyme inactive
Y294A
-
enzyme inactive