Information on EC 6.1.1.7 - Alanine-tRNA ligase

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

EC NUMBER
COMMENTARY
6.1.1.7
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RECOMMENDED NAME
GeneOntology No.
Alanine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla
show the reaction diagram
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-
-
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ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla
show the reaction diagram
kinetic mechanism, AlaRS belongs to the class II of aminoacyl-tRNA ligases due to the position of aminoacylation on the 3'-terminal tRNA ribose, and the topology and tRNAbinding orientation of the active-site protein fold, class II synthetases are rate-limited by a step prior to aminoacyl transfer, the distinct mechanistic signatures of class I versus class II tRNA synthetases ensure rapid turnover of aminoacyl-tRNAs during protein synthesis
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PATHWAY
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
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tRNA charging
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SYSTEMATIC NAME
IUBMB Comments
L-Alanine:tRNAAla ligase (AMP-forming)
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ala-tRNA synthetase
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-
-
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Ala-tRNA synthetase
Q54Y20
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Ala-tRNA synthetase
Q9U6B6
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Ala-tRNA synthetase
-
-
Ala-tRNA synthetase
Q9U022
-
Ala-tRNA synthetase
-
-
Ala-tRNA synthetase
-
-
Alanine transfer RNA synthetase
-
-
-
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Alanine transfer RNA synthetase
Q54Y20
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Alanine transfer RNA synthetase
Q9U6B6
-
Alanine transfer RNA synthetase
-
-
Alanine transfer RNA synthetase
Q9U022
-
Alanine transfer RNA synthetase
-
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Alanine transfer RNA synthetase
-
-
Alanine translase
-
-
-
-
Alanine translase
Q54Y20
-
Alanine translase
Q9U6B6
-
Alanine translase
-
-
Alanine translase
Q9U022
-
Alanine translase
-
-
Alanine translase
-
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Alanine tRNA synthetase
-
-
-
-
Alanine tRNA synthetase
Q54Y20
-
Alanine tRNA synthetase
Q9U6B6
-
Alanine tRNA synthetase
-
-
Alanine tRNA synthetase
Q9U022
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Alanine tRNA synthetase
-
-
Alanine tRNA synthetase
-
-
Alanine--tRNA ligase
-
-
-
-
Alanine-transfer RNA ligase
-
-
-
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Alanine-transfer RNA ligase
Q54Y20
-
Alanine-transfer RNA ligase
Q9U6B6
-
Alanine-transfer RNA ligase
-
-
Alanine-transfer RNA ligase
Q9U022
-
Alanine-transfer RNA ligase
-
-
Alanine-transfer RNA ligase
-
-
alanine-tRNA ligase
Q54Y20
-
alanine-tRNA ligase
Q9U6B6
-
alanine-tRNA ligase
-
-
alanine-tRNA ligase
Q9U022
-
alanine-tRNA ligase
-
-
alanine-tRNA ligase
-
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alanyl tRNA ligase
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alanyl tRNA ligase
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Alanyl-transfer ribonucleate synthetase
-
-
-
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Alanyl-transfer ribonucleate synthetase
Q54Y20
-
Alanyl-transfer ribonucleate synthetase
Q9U6B6
-
Alanyl-transfer ribonucleate synthetase
-
-
Alanyl-transfer ribonucleate synthetase
Q9U022
-
Alanyl-transfer ribonucleate synthetase
-
-
Alanyl-transfer ribonucleate synthetase
-
-
Alanyl-transfer ribonucleic acid synthetase
-
-
-
-
Alanyl-transfer ribonucleic acid synthetase
Q54Y20
-
Alanyl-transfer ribonucleic acid synthetase
Q9U6B6
-
Alanyl-transfer ribonucleic acid synthetase
-
-
Alanyl-transfer ribonucleic acid synthetase
Q9U022
-
Alanyl-transfer ribonucleic acid synthetase
-
-
Alanyl-transfer ribonucleic acid synthetase
-
-
Alanyl-transfer RNA synthetase
-
-
-
-
Alanyl-transfer RNA synthetase
Q54Y20
-
Alanyl-transfer RNA synthetase
Q9U6B6
-
Alanyl-transfer RNA synthetase
-
-
Alanyl-transfer RNA synthetase
Q9U022
-
Alanyl-transfer RNA synthetase
-
-
Alanyl-transfer RNA synthetase
-
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alanyl-tRNA ligase
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alanyl-tRNA synthase
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Alanyl-tRNA synthetase
-
-
-
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Alanyl-tRNA synthetase
-
-
Alanyl-tRNA synthetase
Q54Y20
-
Alanyl-tRNA synthetase
Q9U6B6
-
Alanyl-tRNA synthetase
-
-
Alanyl-tRNA synthetase
Q9U022
-
Alanyl-tRNA synthetase
O58307
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Alanyl-tRNA synthetase
Pyrococcus horikoshii OT-3
O58307
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Alanyl-tRNA synthetase
-
-
Alanyl-tRNA synthetase
-
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AlaRS
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-
-
-
AlaRS
Q9U022
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AlaRS
O58307
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AlaRS
Pyrococcus horikoshii OT-3
O58307
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Synthase, alanyl-transfer ribonucleate
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-
-
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Synthase, alanyl-transfer ribonucleate
Q54Y20
-
Synthase, alanyl-transfer ribonucleate
Q9U6B6
-
Synthase, alanyl-transfer ribonucleate
-
-
Synthase, alanyl-transfer ribonucleate
Q9U022
-
Synthase, alanyl-transfer ribonucleate
-
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Synthase, alanyl-transfer ribonucleate
-
-
additional information
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the enzyme belongs to the MurMN/Fem-ABX family of tRNA-dependent ligases
CAS REGISTRY NUMBER
COMMENTARY
9031-71-4
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
gene alaS
SwissProt
Manually annotated by BRENDA team
gene alaS is nuclear-encoded, mitochondrial isozyme
Q9U6B6
SwissProt
Manually annotated by BRENDA team
K12 strain KL386 that carries the gene on a recombinant pBR322 plasmid
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-
Manually annotated by BRENDA team
overproducing strain
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Manually annotated by BRENDA team
purified recombinant His-tagged enzyme
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Manually annotated by BRENDA team
recombinant wild-type from overexpression in Escherichia coli
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Manually annotated by BRENDA team
wild-type and mutant enzymes with replacement of Lys73 with Gln, Asn, Ala or Glu
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Manually annotated by BRENDA team
wild-type and mutant enzymes with replacement ofcysteine residues, Cys76Ser, Cys290Ser, Cys412Ser, Cys665Ser
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-
Manually annotated by BRENDA team
Escherichia coli overproducing
overproducing strain
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Manually annotated by BRENDA team
expression in Pichia sp.
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-
Manually annotated by BRENDA team
strain OT3, gene PH0574
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3, gene PH0574
SwissProt
Manually annotated by BRENDA team
mitochondrial and cytoplasmic isozymes encoded by a single nuclear gene ALA1
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-
Manually annotated by BRENDA team
strain alphaS288C
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-
Manually annotated by BRENDA team
Saccharomyces cerevisiae alphaS288C
strain alphaS288C
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-
Manually annotated by BRENDA team
strains 159, Pn16
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain HB8
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Manually annotated by BRENDA team
strain HB8, overproduced in Escherichia coli
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
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the relatively modest specificity of the AlaRS editing domain may provide a rationale for the widespread phylogenetic distribution of AlaX free-standing editing domains, thereby contributing a further mechanism to lower concentrations of misacylated tRNAAla
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
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additional information
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the wild-type AlaRS editing domain deacylates Ser-tRNAAla with a kcat/Km of 66 mM/s, equivalent to a rate enhancement of 6000 over the rate of enzyme-independent deacylation but only 12.2fold greater than the rate with Ala-tRNAAla. While the E664A and T567G substitutions only minimally decrease kcat/Km, Q584H, I667E, and C666A AlaRS are more compromised in activity, with decreases in kcat/Km in the range of 6fold, 6.6fold, and 15fold. C666A AlaRS is 1.7fold more active on Ala-tRNAAla relative to Ser-tRNAAl. Deacylation rates of Ser-tRNAAla and Ala-tRNAAla in the absence of enzyme are determined by fitting the progress curves to equations describing a first-order decay
0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.4
7.5
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6.4: about 60% of maximal activity, 7.5: optimum
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
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)
Escherichia coli (strain K12)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sensitive to repeated freezing and thawing
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Zn2+ stabilizes the enzyme
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