6.1.1.7: alanine-tRNA ligase

This is an abbreviated version!
For detailed information about alanine-tRNA ligase, go to the full flat file.

Reaction

Synonyms

AARS2, Ala-tRNA synthetase, ALA1, ALA2, Alanine transfer RNA synthetase, Alanine translase, Alanine tRNA synthetase, Alanine--tRNA ligase, Alanine-transfer RNA ligase, alanine-tRNA ligase, alanyl tRNA ligase, Alanyl-transfer ribonucleate synthetase, Alanyl-transfer ribonucleic acid synthetase, Alanyl-transfer RNA synthetase, alanyl-tRNA ligase, alanyl-tRNA synthase, Alanyl-tRNA synthetase, alanyltRNA synthetase, AlaRS, mitochondrial alanyl-tRNA synthetase, More, mtAlaRS, MurM, MurN, Synthase, alanyl-transfer ribonucleate

ECTree

     6 Ligases

         6.1 Forming carbon-oxygen bonds

             6.1.1 Ligases forming aminoacyl-tRNA and related compounds

                6.1.1.7 alanine-tRNA ligase

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Results	in table
6	Activating Compound
56313	AA Sequence
2	Application
1	CAS Registry Number
29	Cloned(Commentary)
18	Cofactor
9	Crystallization (Commentary)
151	Disease/ Diagnostics
4	Expression
18	General Information
2	General Stability
16	Inhibitors
1	kcat/KM [mM/s]
2	Ki Value [mM]
57	KM Value [mM]
24	Localization
17	Metals/Ions
23	Molecular Weight [Da]
23	Natural Substrates/ Products (Substrates)
159	Organism
4	Pathway
70	PDB ID
14	pH Optimum
1	pH Range
51	Protein Variants
24	Purification (Commentary)
2	Reaction
20	Reaction Type
61	Reference
2	Renatured (Commentary)
8	Source Tissue
11	Specific Activity [micromol/min/mg]
2	Storage Stability
79	Substrates and Products (Substrate)
21	Subunits
176	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
3	Temperature Range [°C]
3	Temperature Stability [°C]
38	Turnover Number [1/s]

KCat KM Value

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KCat KM Value on EC 6.1.1.7 - alanine-tRNA ligase

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

additional information

additional information

Escherichia coli

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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

714234

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