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MetaCyc Protein: AlaS-L-alanine

Gene: alaS Accession Numbers: EG10034 (MetaCyc), b2697, ECK2692

Synonyms: act, ala-act, lovB

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of AlaS-L-alanine = [AlaS][L-alanine]
         alanyl-tRNA synthetase = AlaS (extended summary available)

Citations: [Putney81]

Map Position: [2,817,403 <- 2,820,033]

Unification Links: ASAP:ABE-0008869 , CGSC:1039 , EchoBASE:EB0033 , EcoGene:EG10034 , OU-Microarray:b2697 , PortEco:alaS , RegulonDB:EG10034

Gene-Reaction Schematic: ?

MultiFun Terms: information transfer protein related amino acid -activation
regulation type of regulation transcriptional level repressor

Symmetry: Inverted Repeat

Credits:
Imported from EcoCyc 15-May-2012 by Paley S , SRI International


Subunit of AlaS-L-alanine: alanyl-tRNA synthetase

Synonyms: Act, LovB, AlaS, ala-act

Gene: alaS Accession Numbers: EG10034 (MetaCyc), b2697, ECK2692

Locations: cytosol, membrane

Sequence Length: 876 AAs

Molecular Weight: 96.032 kD (from nucleotide sequence)

Molecular Weight: 95 kD (experimental) [Putney81a]

GO Terms:

Biological Process: GO:0006419 - alanyl-tRNA aminoacylation Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Putney81a]
GO:0006450 - regulation of translational fidelity Inferred from experiment [Beebe08, Beebe03]
GO:0045892 - negative regulation of transcription, DNA-templated Inferred from experiment [Putney81]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11a]
GO:0043039 - tRNA aminoacylation Inferred by computational analysis [GOA01a]
Molecular Function: GO:0001141 - bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from experiment [Putney81]
GO:0002161 - aminoacyl-tRNA editing activity Inferred from experiment [Beebe08, Beebe03]
GO:0004813 - alanine-tRNA ligase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Putney81a]
GO:0008270 - zinc ion binding Inferred from experiment Inferred by computational analysis [GOA06, Miller91a]
GO:0042802 - identical protein binding Inferred from experiment [Lasserre06]
GO:0000049 - tRNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0003676 - nucleic acid binding Inferred by computational analysis [GOA01a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0004812 - aminoacyl-tRNA ligase activity Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016876 - ligase activity, forming aminoacyl-tRNA and related compounds Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]

MultiFun Terms: information transfer protein related amino acid -activation
regulation type of regulation transcriptional level repressor

Unification Links: DIP:DIP-9080N , EcoliWiki:b2697 , Mint:MINT-1266342 , ModBase:P00957 , PR:PRO_000022074 , Pride:P00957 , Protein Model Portal:P00957 , RefSeq:NP_417177 , SMR:P00957 , String:511145.b2697 , Swiss-Model:P00957 , UniProt:P00957

Relationship Links: InterPro:IN-FAMILY:IPR002318 , InterPro:IN-FAMILY:IPR003156 , InterPro:IN-FAMILY:IPR009000 , InterPro:IN-FAMILY:IPR012947 , InterPro:IN-FAMILY:IPR018162 , InterPro:IN-FAMILY:IPR018163 , InterPro:IN-FAMILY:IPR018164 , InterPro:IN-FAMILY:IPR018165 , InterPro:IN-FAMILY:IPR023033 , Panther:IN-FAMILY:PTHR11777:SF6 , PDB:Structure:3HXU , PDB:Structure:3HXV , PDB:Structure:3HXW , PDB:Structure:3HXX , PDB:Structure:3HXY , PDB:Structure:3HXZ , PDB:Structure:3HY0 , PDB:Structure:3HY1 , Pfam:IN-FAMILY:PF01411 , Pfam:IN-FAMILY:PF02272 , Pfam:IN-FAMILY:PF07973 , Prints:IN-FAMILY:PR00980 , Prosite:IN-FAMILY:PS50860 , Smart:IN-FAMILY:SM00863

Summary:
Alanyl-tRNA synthetase (AlaRS) 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. AlaRS belongs to the Class II aminoacyl tRNA synthetases, which share three regions of homology [Eriani90, Cusack91].

AlaRS was seen as a homotetramer in solution [Putney81a]. Later experiments determined that AlaRS exists in an equilibrium between a homodimeric and a homodecameric state, depending on temperature [Sood96, Sood97]. The enzyme contains one molecule of zinc per AlaS polypeptide [Miller91a]; zinc binds cooperatively and induces a conformational change in AlaRS [Wu94, Sood99]. Zinc is important for tRNA recognition [Miller92].

Specificity determinants within tRNAAla that are important for recognition by AlaRS have been identified [Park88a, Gabriel96, McClain96, McClain99, Pleiss00, Wolfson02, Beuning02]. A single nucleotide base pair in the acceptor helix of tRNAAla, G3-U70, is necessary and sufficient for aminoacylation of that tRNA with alanine [Hou88, McClain88, McClain88a, Hou89, MusierForsyth92, Beuning97, Chang99]. A mutation in alaS which compensates for a mutant tRNAAla containing a G3-C70 base pair has been isolated [Miller91b]. Discrimination of the G3-U70 base pair maps to a 76 amino acid region outside the catalytic center of AlaRS [Buechter95]. The nucleotide at position 73 modulates the efficiency of the transfer step of aminoacylation [Shi90, Shi91, Fischer99, Nagan00].

Specificity determinants and residues within AlaRS that are important for catalytic activity have been investigated [Park90, Ribas98]. An N-terminal 461 amino acid fragment of the AlaS polypeptide was shown to complement a temperature-sensitive alaS allele in vivo; the C-terminal portion of the enzyme appears to be dispensable for catalytic activity, but is required for formation of the tetramer [Putney81a, Putney81b, Jasin83, Jasin85]. Mutagenesis of an N-terminal domain peptide reveals residues that increase catalytic activity of the fragment [Ho85]. A central region of AlaRS is essential for interaction with alanine-specific tRNA [Regan87]. Site-directed mutagenesis has identified the Arg69 residue within motif 2 [Lu94, Davis94], the Cys665 residue [Wu94a] and the Asp235 residue [Shi94a] as important for catalysis. The Lys73 residue is important for recognition of tRNAAla [Hill89, Filley93].

Single turnover kinetics experiments showed that a step prior to aminoacyl transfer is rate limiting [Zhang06a]. Kinetic parameters for binding of AlaRS to tmRNA have been determined [Barends00].

The central domain of AlaRS is the editing domain. Many aminoacyl-tRNA synthetases have been shown to have editing functions. AlaRS misactivates glycine and serine, but has a pre-transfer editing function, hydrolyzing the non-cognate amino acid before transfer to tRNAAla, and a post-transfer editing function that deacetylates mischarged tRNAAla [Tsui81, Beebe03a]. A series of crystal structures, together with kinetic analysis and mutagenesis, has allowed elucidation of the basis for recognition of alanine by AlaRS and provides a structural and evolutionary explanation for the interaction with serine [Guo09]. The covalently continuous two-domain structure of the tRNA is required to enable editing [Beebe03a]. The editing domain alone is able to specifically recognize mischarged tRNAAla, utilizing the same discriminator base pair within the tRNA as the aminoacylation domain [Beebe08].

The C-terminal domain (C-Ala) plays a role in activating the catalytic sites of the N-terminal domain [Jasin84]. C-Ala represents the major tRNA binding module of AlaRS [Guo09a]; this tRNA binding activity is required for efficient editing activity by the central editing domain [Beebe08]. The C-Ala domain serves to bring the aminoacylation and editing domains of AlaRS together to bind to the acceptor stem of tRNAAla [Guo09a].

AlaRS represses transcription of the alaS gene by binding to a region flanking the transcription start site, and thus autoregulates its own expression. The autoregulatory effect depends on the concentration of alanine, with higher concentrations leading to lower levels of alaS transcription. At physiological levels of AlaRS, repression of alaS transcription is solely mediated by alanine levels [Putney81].

The alaS21 allele leads to increased resistance to novobiocin [Jovanovic99]. Mutations in ribosomal proteins S5 and S20 partially suppresses the temperature sensitive growth defect of an alaS mutation [Wittmann74]. The mechanism of suppression is thought to be a reduction in the rate of polypeptide synthesis [Buckel76].

Reviews: [Ataide06, Ibba00, Hou89a, Miller92a]

History:
10/20/97 Gene b2697 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10034; confirmed by SwissProt match.


References

Ataide06: Ataide SF, Ibba M (2006). "Small molecules: big players in the evolution of protein synthesis." ACS Chem Biol 1(5);285-97. PMID: 17163757

Barends00: Barends S, Wower J, Kraal B (2000). "Kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli." Biochemistry 39(10);2652-8. PMID: 10704215

Beebe03: Beebe K, Ribas De Pouplana L, Schimmel P (2003). "Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability." EMBO J 22(3);668-75. PMID: 12554667

Beebe03a: Beebe K, Merriman E, Schimmel P (2003). "Structure-specific tRNA determinants for editing a mischarged amino acid." J Biol Chem 278(46);45056-61. PMID: 12949076

Beebe08: Beebe K, Mock M, Merriman E, Schimmel P (2008). "Distinct domains of tRNA synthetase recognize the same base pair." Nature 451(7174);90-3. PMID: 18172502

Beuning02: Beuning PJ, Nagan MC, Cramer CJ, Musier-Forsyth K, Gelpi JL, Bashford D (2002). "Efficient aminoacylation of the tRNA(Ala) acceptor stem: dependence on the 2:71 base pair." RNA 8(5);659-70. PMID: 12022232

Beuning97: Beuning PJ, Yang F, Schimmel P, Musier-Forsyth K (1997). "Specific atomic groups and RNA helix geometry in acceptor stem recognition by a tRNA synthetase." Proc Natl Acad Sci U S A 94(19);10150-4. PMID: 9294178

Buckel76: Buckel P, Piepersberg W, Bock A (1976). "Suppression of temperature-sensitive aminoacyl-tRNA synthetase mutations by ribosomal mutations: a possible mechanism." Mol Gen Genet 149(1);51-61. PMID: 796671

Buechter95: Buechter DD, Schimmel P (1995). "Minor groove recognition of the critical acceptor helix base pair by an appended module of a class II tRNA synthetase." Biochemistry 34(18);6014-9. PMID: 7742303

Chang99: Chang KY, Varani G, Bhattacharya S, Choi H, McClain WH (1999). "Correlation of deformability at a tRNA recognition site and aminoacylation specificity." Proc Natl Acad Sci U S A 96(21);11764-9. PMID: 10518524

Cusack91: Cusack S, Hartlein M, Leberman R (1991). "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases." Nucleic Acids Res 19(13);3489-98. PMID: 1852601

Davis94: Davis MW, Buechter DD, Schimmel P (1994). "Functional dissection of a predicted class-defining motif in a class II tRNA synthetase of unknown structure." Biochemistry 33(33);9904-11. PMID: 8060998

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

Filley93: Filley SJ, Hill KA (1993). "Amino acid substitutions at position 73 in motif 2 of Escherichia coli alanyl-tRNA synthetase." Arch Biochem Biophys 307(1);46-51. PMID: 8239663

Fischer99: Fischer AE, Beuning PJ, Musier-Forsyth K (1999). "Identification of discriminator base atomic groups that modulate the alanine aminoacylation reaction." J Biol Chem 274(52);37093-6. PMID: 10601268

Gabriel96: Gabriel K, Schneider J, McClain WH (1996). "Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase." Science 271(5246);195-7. PMID: 8539617

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Guo09: Guo M, Chong YE, Shapiro R, Beebe K, Yang XL, Schimmel P (2009). "Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma." Nature 462(7274);808-12. PMID: 20010690

Guo09a: Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P (2009). "The C-Ala domain brings together editing and aminoacylation functions on one tRNA." Science 325(5941);744-7. PMID: 19661429

Hill89: Hill K, Schimmel P (1989). "Evidence that the 3' end of a tRNA binds to a site in the adenylate synthesis domain of an aminoacyl-tRNA synthetase." Biochemistry 28(6);2577-86. PMID: 2543446

Ho85: Ho C, Jasin M, Schimmel P (1985). "Amino acid replacements that compensate for a large polypeptide deletion in an enzyme." Science 229(4711);389-93. PMID: 3892692

Hou88: Hou YM, Schimmel P (1988). "A simple structural feature is a major determinant of the identity of a transfer RNA." Nature 333(6169);140-5. PMID: 3285220

Hou89: Hou YM, Schimmel P (1989). "Modeling with in vitro kinetic parameters for the elaboration of transfer RNA identity in vivo." Biochemistry 28(12);4942-7. PMID: 2548595

Hou89a: Hou YM, Francklyn C, Schimmel P (1989). "Molecular dissection of a transfer RNA and the basis for its identity." Trends Biochem Sci 14(6);233-7. PMID: 2669241

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

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jasin83: Jasin M, Regan L, Schimmel P (1983). "Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase." Nature 306(5942);441-7. PMID: 6358898

Jasin84: Jasin M, Regan L, Schimmel P (1984). "Dispensable pieces of an aminoacyl tRNA synthetase which activate the catalytic site." Cell 36(4);1089-95. PMID: 6200234

Jasin85: Jasin M, Regan L, Schimmel P (1985). "Two mutations in the dispensable part of alanine tRNA synthetase which affect the catalytic activity." J Biol Chem 260(4);2226-30. PMID: 3882689

Jovanovic99: Jovanovic M, Lilic M, Janjusevic R, Jovanovic G, Savic DJ, Milija J (1999). "tRNA synthetase mutants of Escherichia coli K-12 are resistant to the gyrase inhibitor novobiocin." J Bacteriol 181(9);2979-83. PMID: 10217798

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lu94: Lu Y, Hill KA (1994). "The invariant arginine in motif 2 of Escherichia coli alanyl-tRNA synthetase is important for catalysis but not for substrate binding." J Biol Chem 269(16);12137-41. PMID: 8163518

McClain88: McClain WH, Foss K (1988). "Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end." Science 240(4853);793-6. PMID: 2452483

McClain88a: McClain WH, Chen YM, Foss K, Schneider J (1988). "Association of transfer RNA acceptor identity with a helical irregularity." Science 242(4886);1681-4. PMID: 2462282

McClain96: McClain WH, Gabriel K, Schneider J (1996). "Specific function of a G.U wobble pair from an adjacent helical site in tRNA(Ala) during recognition by alanyl-tRNA synthetase." RNA 2(2);105-9. PMID: 8601277

McClain99: McClain WH, Jou YY, Bhattacharya S, Gabriel K, Schneider J (1999). "The reliability of in vivo structure-function analysis of tRNA aminoacylation." J Mol Biol 290(2);391-409. PMID: 10390340

Miller91a: Miller WT, Hill KA, Schimmel P (1991). "Evidence for a "cysteine-histidine box" metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase." Biochemistry 30(28);6970-6. PMID: 1712632

Miller91b: Miller WT, Hou YM, Schimmel P (1991). "Mutant aminoacyl-tRNA synthetase that compensates for a mutation in the major identity determinant of its tRNA." Biochemistry 30(10);2635-41. PMID: 2001352

Miller92: Miller WT, Schimmel P (1992). "A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition." Proc Natl Acad Sci U S A 89(6);2032-5. PMID: 1549561

Miller92a: Miller WT, Schimmel P (1992). "A metal-binding motif implicated in RNA recognition by an aminoacyl-tRNA synthetase and by a retroviral gene product." Mol Microbiol 6(10);1259-62. PMID: 1379318

MusierForsyth92: Musier-Forsyth K, Schimmel P (1992). "Functional contacts of a transfer RNA synthetase with 2'-hydroxyl groups in the RNA minor groove." Nature 357(6378);513-5. PMID: 1608452

Nagan00: Nagan MC, Beuning P, Musier-Forsyth K, Cramer CJ (2000). "Importance of discriminator base stacking interactions: molecular dynamics analysis of A73 microhelix(Ala) variants." Nucleic Acids Res 28(13);2527-34. PMID: 10871402

Park88a: Park SJ, Schimmel P (1988). "Evidence for interaction of an aminoacyl transfer RNA synthetase with a region important for the identity of its cognate transfer RNA." J Biol Chem 263(32);16527-30. PMID: 3053691

Park90: Park SJ, Miller WT, Schimmel P (1990). "Synthetic peptide model of an essential region of an aminoacyl-tRNA synthetase." Biochemistry 29(39);9212-8. PMID: 2271589

Pleiss00: Pleiss JA, Wolfson AD, Uhlenbeck OC (2000). "Mapping contacts between Escherichia coli alanyl tRNA synthetase and 2' hydroxyls using a complete tRNA molecule." Biochemistry 39(28);8250-8. PMID: 10889033

Putney81: Putney SD, Schimmel P (1981). "An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription." Nature 291(5817);632-5. PMID: 6264314

Putney81a: Putney SD, Sauer RT, Schimmel PR (1981). "Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits." J Biol Chem 256(1);198-204. PMID: 7005211

Putney81b: Putney SD, Royal NJ, Neuman de Vegvar H, Herlihy WC, Biemann K, Schimmel P (1981). "Primary structure of a large aminoacyl-tRNA synthetase." Science 213(4515);1497-501. PMID: 7025207

Regan87: Regan L, Bowie J, Schimmel P (1987). "Polypeptide sequences essential for RNA recognition by an enzyme." Science 235(4796);1651-3. PMID: 2435005

Ribas98: Ribas de Pouplana L, Buechter D, Sardesai NY, Schimmel P (1998). "Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA-binding domains." EMBO J 17(18);5449-57. PMID: 9736622

Shi90: Shi JP, Francklyn C, Hill K, Schimmel P (1990). "A nucleotide that enhances the charging of RNA minihelix sequence variants with alanine." Biochemistry 29(15);3621-6. PMID: 1692733

Shi91: Shi JP, Schimmel P (1991). "Aminoacylation of alanine minihelices. "Discriminator" base modulates transition state of single turnover reaction." J Biol Chem 266(5);2705-8. PMID: 1704363

Shi94a: Shi JP, Musier-Forsyth K, Schimmel P (1994). "Region of a conserved sequence motif in a class II tRNA synthetase needed for transfer of an activated amino acid to an RNA substrate." Biochemistry 33(17);5312-8. PMID: 8172905

Sood96: Sood SM, Slattery CW, Filley SJ, Wu MX, Hill KA (1996). "Further characterization of Escherichia coli alanyl-tRNA synthetase." Arch Biochem Biophys 328(2);295-301. PMID: 8645007

Sood97: Sood SM, Hill KA, Slattery CW (1997). "Stability of Escherichia coli alanyl-tRNA synthetase quaternary structure under increased pressure." Arch Biochem Biophys 346(2);322-3. PMID: 9343380

Sood99: Sood SM, Wu MX, Hill KA, Slattery CW (1999). "Characterization of zinc-depleted alanyl-tRNA synthetase from Escherichia coli: role of zinc." Arch Biochem Biophys 368(2);380-4. PMID: 10441391

Tsui81: Tsui WC, Fersht AR (1981). "Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli." Nucleic Acids Res 9(18);4627-37. PMID: 6117825

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

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

Wittmann74: Wittmann HG, Stoffler G (1974). "Altered S5 and S20 ribosomal proteins in revertants of an alanyl-tRNA synthetase mutant of Escherichia coli." Mol Gen Genet 134(3);225-36. PMID: 4280505

Wolfson02: Wolfson AD, Uhlenbeck OC (2002). "Modulation of tRNAAla identity by inorganic pyrophosphatase." Proc Natl Acad Sci U S A 99(9);5965-70. PMID: 11983895

Wu94: Wu MX, Filley SJ, Hill KA (1994). "Cooperative binding of zinc to an aminoacyl-tRNA synthetase." Biochem Biophys Res Commun 201(3);1079-83. PMID: 8024549

Wu94a: Wu MX, Filley SJ, Xiong J, Lee JJ, Hill KA (1994). "A cysteine in the C-terminal region of alanyl-tRNA synthetase is important for aminoacylation activity." Biochemistry 33(40);12260-6. PMID: 7918446

Zhang06a: Zhang CM, Perona JJ, Ryu K, Francklyn C, Hou YM (2006). "Distinct kinetic mechanisms of the two classes of Aminoacyl-tRNA synthetases." J Mol Biol 361(2);300-11. PMID: 16843487


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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