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
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: asparaginyl-tRNA synthetase



Gene: asnS Accession Numbers: EG10094 (EcoCyc), b0930, ECK0921

Synonyms: lcs, tss

Regulation Summary Diagram: ?

Subunit composition of asparaginyl-tRNA synthetase = [AsnS]2
         asparaginyl-tRNA synthetase = AsnS

Summary:
Asparaginyl-tRNA synthetase (AsnRS) is a member of the family of aminoacyl-tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. The reaction is driven by ATP hydrolysis. AsnRS belongs to the Class II aminoacyl tRNA synthetases, which share three regions of homology [Eriani90].

AsnRS is a dimer in solution [Anselme89, Aoki92]. Analysis of mutants suggests that the Y426 residue is involved in ATP binding [Anselme91]; a P231L mutation, which is located in the conserved motif 2 of class II aminoacyl-tRNA synthetases, leads to increases in the Km for asparagine and ATP [Madern92].

Review: [Ibba00]

Locations: cytosol

Map Position: [986,808 <- 988,208] (21.27 centisomes)
Length: 1401 bp / 466 aa

Molecular Weight of Polypeptide: 52.57 kD (from nucleotide sequence), 54 kD (experimental) [Anselme89 ]

Unification Links: ASAP:ABE-0003162 , CGSC:993 , EchoBASE:EB0092 , EcoGene:EG10094 , EcoliWiki:b0930 , Mint:MINT-1319001 , OU-Microarray:b0930 , PortEco:asnS , PR:PRO_000022170 , Pride:P0A8M0 , Protein Model Portal:P0A8M0 , RefSeq:NP_415450 , RegulonDB:EG10094 , SMR:P0A8M0 , String:511145.b0930 , UniProt:P0A8M0

Relationship Links: InterPro:IN-FAMILY:IPR002312 , InterPro:IN-FAMILY:IPR004364 , InterPro:IN-FAMILY:IPR004365 , InterPro:IN-FAMILY:IPR004522 , InterPro:IN-FAMILY:IPR006195 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR018150 , Panther:IN-FAMILY:PTHR22594 , Panther:IN-FAMILY:PTHR22594:SF6 , Pfam:IN-FAMILY:PF00152 , Pfam:IN-FAMILY:PF01336 , Prints:IN-FAMILY:PR01042 , Prosite:IN-FAMILY:PS50862

In Paralogous Gene Group: 225 (4 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006418 - tRNA aminoacylation for protein translation Inferred from experiment Inferred by computational analysis [GOA01, Madern92]
GO:0006421 - asparaginyl-tRNA aminoacylation Inferred from experiment Inferred by computational analysis [GOA01, Madern92]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004816 - asparagine-tRNA ligase activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Madern92]
GO:0005524 - ATP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Anselme91]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0003676 - nucleic acid binding Inferred by computational analysis [GOA01]
GO:0004812 - aminoacyl-tRNA ligase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA01]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer protein related amino acid -activation

Essentiality data for asnS knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Last-Curated ? 19-Jun-2006 by Keseler I , SRI International


Enzymatic reaction of: asparaginyl-tRNA synthetase

Synonyms: AsnRS

EC Number: 6.1.1.22

tRNAasn + L-asparagine + ATP + H+ <=> L-asparaginyl-tRNAasn + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: tRNA charging

Summary:
Kinetic parameters of purified wild type and mutant enzymes were measured under various conditions [Madern92]. Reported below are the values measured for the aminoacylation reaction at 37° C.

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
L-asparagine
15.3, 32.3
1.6
[Anselme91, BRENDA14]
L-asparagine
15.0, 29.0, 32.0
2.8
[Madern92, BRENDA14]
ATP
76.0
[Anselme91, BRENDA14]
ATP
500.0, 76.0
2.2
[Madern92, BRENDA14]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Anselme89, Link97, UniProt11]
UniProt: Removed.
Chain 2 -> 466
[UniProt09]
UniProt: Asparaginyl-tRNA synthetase;
Extrinsic-Sequence-Variant 231
[UniProt10]
Alternate sequence: P → L; UniProt: (in temperature-sensitive mutant HO202);
Mutagenesis-Variant 426
[UniProt10]
Alternate sequence: Y → S; UniProt: 15-fold increase in Km for ATP;
Alternate sequence: Y → F; UniProt: No effect;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0930 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10094; confirmed by SwissProt match.


References

Anselme89: Anselme J, Hartlein M (1989). "Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase." Gene 84(2);481-5. PMID: 2693216

Anselme91: Anselme J, Hartlein M (1991). "Tyr-426 of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding." FEBS Lett 280(1);163-6. PMID: 2009959

Aoki92: Aoki H, Yaworsky PJ, Patel SD, Margolin-Brzezinski D, Park KS, Ganoza MC (1992). "The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316." Eur J Biochem 209(2);511-21. PMID: 1425658

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Eriani90: Eriani G, Delarue M, Poch O, Gangloff J, Moras D (1990). "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs." Nature 347(6289);203-6. PMID: 2203971

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Ibba00: Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis." Annu Rev Biochem 69;617-50. PMID: 10966471

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

Madern92: Madern D, Anselme J, Hartlein M (1992). "Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP." FEBS Lett 299(1);85-9. PMID: 1544480

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, biocyc13.