Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 6.1.1.7

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Macromolecule Reactions Polynucleotide-Reactions RNA-Reactions tRNA-Reactions tRNA-Charging-Reactions

EC Number: 6.1.1.7

Enzymes and Genes:
alanyl-tRNA synthetase and DNA-binding transcriptional repressor Inferred from experiment : alaS ( Escherichia coli K-12 substr. MG1655 )

In Pathway: tRNA charging

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: alanine—tRNA ligase

Enzyme Commission Synonyms: alanyl-tRNA synθse, alanyl-transfer ribonucleate synθse, alanyl-transfer RNA synθse, alanyl-transfer ribonucleic acid synθse, alanine-transfer RNA ligase, alanine transfer RNA synθse, alanine tRNA synθse, alanine translase, alanyl-transfer ribonucleate synthase, AlaRS, Ala-tRNA synθse

Citations: [HOLLEY59, WEBSTER61]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R03038 , Rhea:12540

Relationship Links: BRENDA:EC:6.1.1.7 , ENZYME:EC:6.1.1.7 , IUBMB-ExplorEnz:EC:6.1.1.7 , UniProt:RELATED-TO:O27718 , UniProt:RELATED-TO:O34526 , UniProt:RELATED-TO:O50189 , UniProt:RELATED-TO:O51238 , UniProt:RELATED-TO:O58035 , UniProt:RELATED-TO:O67323 , UniProt:RELATED-TO:O83980 , UniProt:RELATED-TO:P00957 , UniProt:RELATED-TO:P21894 , UniProt:RELATED-TO:P24075 , UniProt:RELATED-TO:P27866 , UniProt:RELATED-TO:P35029 , UniProt:RELATED-TO:P40825 , UniProt:RELATED-TO:P43815 , UniProt:RELATED-TO:P47534 , UniProt:RELATED-TO:P49588 , UniProt:RELATED-TO:P50475 , UniProt:RELATED-TO:P56452 , UniProt:RELATED-TO:P75368 , UniProt:RELATED-TO:Q9CEW0 , UniProt:RELATED-TO:Q9JTG4 , UniProt:RELATED-TO:Q9PI05 , UniProt:RELATED-TO:Q9X1B6 , UniProt:RELATED-TO:Q9Z714 , UniProt:RELATED-TO:Q9ZCA4 , UniProt:RELATED-TO:Q9ZJY5 , UniProt:RELATED-TO:Q48976 , UniProt:RELATED-TO:Q57984


References

HOLLEY59: HOLLEY RW, GOLDSTEIN J (1959). "An alanine-dependent, ribonuclease-inhibited conversion of adenosine 5'-phosphate to adenosine triphosphate. II. Reconstruction of the system from purified components." J Biol Chem 234(7);1765-8. PMID: 13672960

WEBSTER61: WEBSTER GC (1961). "Isolation of an alanine-activating enzyme from pig liver." Biochim Biophys Acta 49;141-52. PMID: 13783653


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, biocyc13.