Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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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 Mon Dec 22, 2014, BIOCYC13A.