Metabolic Modeling Tutorial
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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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Aquifex aeolicus VF5 Reaction: 6.1.1.10

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: 6.1.1.10

Enzymes and Genes:
methionyl-tRNA synthetase subunit beta : metG'
methionyl-tRNA synthetase subunit alpha : metG

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: methionine—tRNA ligase

Enzyme Commission Synonyms: methionyl-tRNA synθse, methionyl-transfer ribonucleic acid synθse, methionyl-transfer ribonucleate synθse, methionyl-transfer RNA synθse, methionine translase, MetRS

Enzyme Commission Summary:
In those organisms producing N-formylmethionyl-tRNAfMet for translation initiation, this enzyme also recognizes the initiator tRNAfMet and catalyses the formation of L-methionyl-tRNAfMet, the substrate for EC 2.1.2.9, methionyl-tRNA formyltransferase.

Citations: [Lee92a]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:6.1.1.10 , ENZYME:EC:6.1.1.10 , IUBMB-ExplorEnz:EC:6.1.1.10

Credits:
Imported from MetaCyc 08-Aug-2014 by Subhraveti P , SRI International


References

Lee92a: Lee CP, Dyson MR, Mandal N, Varshney U, Bahramian B, RajBhandary UL (1992). "Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase." Proc Natl Acad Sci U S A 89(19);9262-6. PMID: 1409632


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Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc13.