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Ligand L-alanyl-tRNA

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for L-alanyl-tRNA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.10

L-alanyl-tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine

736928

-

2.3.2.10

L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine

487792, 659068, 660520

-

2.3.2.10

2 entries

2.3.2.11

L-alanyl-tRNAAla + phosphatidylglycerol = tRNAAla + 3-O-L-alanyl-1-O-phosphatidylglycerol

705780, 705781, 737171

-

2.3.2.B16

L-tryptophanyl-tRNATrp + L-alanyl-tRNAAla = tRNATrp + tRNAAla + cyclo(L-tryptophanyl-L-alanyl)

758682

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.1.1.15

ATP + L-alanine + tRNAPro = AMP + diphosphate + L-alanyl-tRNAPro

-

-

6.1.1.7

ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla

651165, 649422, 649960, 650000, , 651649, 653639

-

Substrate in Enzyme-catalyzed Reactions (16 results)

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Show Substrate (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.10

L-alanyl-tRNA(Ala) + UDP-N-acetylmuramoyl-pentapeptide containing L-lysine = ?

487793

-

2.3.2.10

L-alanyl-tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine

736928

-

2.3.2.10

L-alanyl-tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine

487793, 659068, 660520, 487792

-

2.3.2.10

L-alanyl-tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNASer + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine

487793

-

2.3.2.11

L-alanyl-tRNA + 1,2-dicaproyl-sn-glycero-3-phospho-(1'-rac-glycerol) = ?

720495

-

2.3.2.11

L-alanyl-tRNA + 1,2-diphytanoyl-sn-glycero-3-phospho-(1'-rac-glycerol) = ?

719738, 720495

-

2.3.2.11

L-alanyl-tRNA + 1-oleoyl-2-hydroxy-sn-glycero-3-phospho-(1'-rac-glycerol) = ?

720495

-

2.3.2.11

L-alanyl-tRNAAla + phosphatidylglycerol = tRNAAla + 3-O-L-alanyl-1-O-phosphatidylglycerol

705780, 705781, 719738, 737171, 720495, 487794

-

2.3.2.10

4 entries

2.3.2.11

4 entries

2.3.2.16

L-alanyl-tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-D-Ala = tRNA(E.coli) + UDP-MurNAc-Ala-D-Glu-(N6-L-Ala)Lys-D-Ala-D-Ala

704401

-

2.3.2.B1

ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanyl-L-alanyl-gamma-D-glutamyl-L-lysine + alanyl-tRNA = ? + tRNA

712366

-

2.3.2.B1

ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA = ? + tRNA

712366

-

2.3.2.B1

UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA

712366

-

2.3.2.B1

3 entries

2.3.2.B16

L-tryptophanyl-tRNATrp + L-alanyl-tRNAAla = tRNATrp + tRNAAla + cyclo(L-tryptophanyl-L-alanyl)

758682

-

2.3.2.B2

UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + L-alanyl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl-L-alanyl)-D-alanyl-D-alanine + tRNA

712365

-

2.3.2.B2

UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + L-alanyl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryll-L-alanyl)-D-alanyl-D-alanine + tRNA

712365

-

2.3.2.B2

2 entries

3.1.1.29

Ala-tRNA + H2O = Ala + tRNA

648114

-

Product in Enzyme-catalyzed Reactions (10 results)

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Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.1.1.15

ATP + L-alanine + tRNAPro = AMP + diphosphate + L-alanyl-tRNAPro

, 652154, 652299, 650167

-

6.1.1.20

ATP + L-alanine + tRNAPhe = AMP + diphosphate + L-alanyl-tRNAPhe

-

-

6.1.1.6

ATP + L-alanine + tRNALys = AMP + L-alanyl-tRNALys + diphosphate

649906

-

6.1.1.7

ATP + L-alanine + tmRNA = AMP + diphosphate + L-alanyl-tmRNA

651165, 649960

-

6.1.1.7

ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla

651165, 511, 512, 513, 514, 515, 520, 524, 649422, 649960, 650000, , 516, 519, 11, 521, 651649, 92, 156, 525, 653639, 510, 517

-

6.1.1.7

ATP + L-alanine + dual specific tRNAPhe = AMP + diphosphate + L-alanyl-tRNAPhe

650000

-

6.1.1.7

ATP + L-alanine + dual specific tRNAPhe(17) = AMP + diphosphate + L-alanyl-tRNAPhe(17)

650000

-

6.1.1.7

ATP + L-alanine + dual specific tRNAPhe(38) = AMP + diphosphate + L-alanyl-tRNAPhe(38)

650000

-

6.1.1.7

ATP + L-alanine + dual specific tRNAPhe(57) = AMP + diphosphate + L-alanyl-tRNAPhe(57)

650000

-

6.1.1.7

ATP + L-alanine + tRNAPyl = AMP + diphosphate + L-alanyl-tRNAPyl

-

-

6.1.1.7

7 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (5 results)

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Show Turnover Number (5 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.3.2.10

0.183

-

recombinant mutant D109N

487793

2.3.2.10

0.917

-

recombinant mutant E320Q

487793

2.3.2.10

11

-

recombinant wild-type

487793

2.3.2.10

26.7

-

pH 7.5, 30°C

659068

2.3.2.10

4 entries

2.3.2.B1

0.021

-

pH 7.6, 37°C

712366

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.2.10

0.0017

-

pH 7.5, 30°C

659068

2.3.2.10

0.015

-

Ala-tRNAAla from E. coli, recombinant wild-type

487793

2.3.2.10

0.054

-

Ala-tRNAAla from E. coli, recombinant mutant E320Q

487793

2.3.2.10

0.061

-

Ala-tRNAAla from E. coli, recombinant mutant D109N

487793

2.3.2.10

4 entries

2.3.2.B1

0.00021

-

pH 7.6, 37°C

712366

References & Links

Literature References (42)

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Show Reference (42 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

11

-

Purification of tyrosine:tRNA ligase, valine:tRNA ligase, alanine:tRNA ligase, and isoleucine:tRNA ligase from Saccharomyces cerevisiae alphaS288C

1974

Bhanot, O.S.; Kucan, Z.; Aoyagi, S.; Lee, F.C.; Chambers, R.W.

Methods Enzymol.

29E

547-576

92

6849897

Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes

1983

Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.

Biochemistry

22

1934-1941

156

6706990

Glycyl- and alanyl-tRNA synthetases from Bombyx mori. Purification and properties

1984

Dignam, S.S.; Dignam, J.D.

J. Biol. Chem.

259

4043-4048

510

9207019

A biologically active 53 kDa fragment of overproduced alanyl-tRNA synthetase from Thermus thermophilus HB8 specifically interacts with tRNAAla acceptor helix

1997

Lechler, A.; Martin, A.; Zuleeg, T.; Limmer, S.; Kreutzer, R.

Nucleic Acids Res.

25

2737-2744

511

2407064

Alanine transfer synthetase. Structure-function relationships and molecular recognition of transfer RNA

1990

Schimmel, P.

Adv. Enzymol. Relat. Areas Mol. Biol.

63

233-270

512

8645007

Further characterization of Escherichia coli alanyl-tRNA synthetase

1996

Sood, S.M.; Slattery, C.W.; Filley, S.J.; Wu, M.X.; Hill, K.A.

Arch. Biochem. Biophys.

328

295-301

513

7654687

Human alanyl-tRNA synthetase. Conservation in evolution of catalytic core and microhelix recognition

1995

Shiba, K.; Ripmaster, T.; Suzuki, N.; Nichols, R.; Plotz, P.; Noda, T.; Schimmel, P.

Biochemistry

34

10340-10349

514

8239663

Amino acid substitutions at position 73 in motif 2 of Escherichia coli alanyl-tRNA synthetase

1993

Filley, S.J.; Hill, K.A.W.

Arch. Biochem. Biophys.

307

46-51

515

7918446

A cysteine in the C-terminal region of alanyl-tRNA synthetase is important for aminoacylation activity

1994

Wu, M.X.; Filley, S.J.; Xiong, J.; Lee, J.J.; Hill, K.A.W.

Biochemistry

33

12260-12266

516

13672960

An alanine-dependent, ribonuclease-inhibited conversion of adenosine 5'-phosphate to adenosine triphosphate

1959

Holley, R.W.; Goldstein, J.

J. Biol. Chem.

234

1765-1768

517

13783653

Isolation of an alanine-activating enzyme from pig liver

1961

Webster, G.C.

Biochim. Biophys. Acta

49

141-152

519

901482

Isolation of an activator macromolecule for alanyl-tRNA synthetase from rat liver

1977

Hilderman, R.H.

Biochem. Biophys. Res. Commun.

77

509-517

520

7005211

Purification and properties of alanine tRNA synthetase from Escherichia coli

1981

Putney, S.D.; Sauer, R.T.; Schimmmel, P.R.

J. Biol. Chem.

256

198-204

521

7013809

Purification and some properties of alanyl- and leucyl-tRNA synthetases from baker's yeast

1981

Kern, D.; Giege, R.; Ebel, J.P.

Biochim. Biophys. Acta

653

83-90

524

6091553

Reactions of the sulfhydryl groups of alanyl-tRNA synthetase

1984

Chen, Z.Q.; Park Kim, J.J.; Lai, C.S.; Mehler, A.H.

Arch. Biochem. Biophys.

233

611-616

525

6570482

Purification and properties of alanyl-tRNA synthetase from Bombyx mori. A monomeric enzyme

1984

Nishio, K.; Kawakami, M.

J. Biochem.

96

1867-1874

487792

-

Biosynthesis of the peptidoglycan of bacterial cell walls

1970

Plapp, R.; Strominger, J.L.

J. Biol. Chem.

245

3673-3682

487793

12679335

Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase)

2003

Hegde, S.S.; Blanchard, J.S.

J. Biol. Chem.

278

22861-22867

487794

4297471

Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. II. Specificity of alanyl phosphatidylglycerol synthetase

1968

Gould, R.M.; Thornton, M.P.; Liepkalns, V.; Lennarz, W.J.

J. Biol. Chem.

243

3096-3104

648114

-

Purification and characterization of an aminoacyl-tRNA hydrolase from the filamentous fungus Fusarium culmorum

1986

Ferreiro, C.; Heredia, C.F.

Biochim. Biophys. Acta

882

410-418

649422

10441391

Characterization of zinc-depleted alanyl-tRNA synthetase from Escherichia coli: role of zinc

1999

Sood, S.M.; Wu, M.X.; Hill, K.A.; Slattery, C.W.

Arch. Biochem. Biophys.

368

380-384

649906

10387054

Misacylation of tRNALys with noncognate amino acids by lysyl-tRNA synthetase

1999

Jakubowski, H.

Biochemistry

38

8088-8093

649960

10704215

kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli

2000

Barends, S.; Wower, J.; Kraal, B.

Biochemistry

39

2652-2658

650000

10889033

Mapping contacts between Escherichia coli alanyl tRNA synthetase and 2' hydroxyls using a complete tRNA molecule

2000

Pleiss, J.A.; Wolfson, A.D.; Uhlenbeck, O.C.

Biochemistry

39

8250-8258

650167

12033945

Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing

2002

Wong, F.C.; Beuning, P.J.; Nagan, M.; Shiba, K.; Musier-Forsyth, K.

Biochemistry

41

7108-7115

651165

12542696

tmRNA from Thermus thermophilus. Interaction with alanyl-tRNA synthetase and elongation factor Tu

2003

Stepanov, V.G.; Nyborg, J.

Eur. J. Biochem.

270

463-475

651649

10601222

CDC64 encodes cytoplasmic alanyl-tRNA synthetase, Ala1p, of Saccharomyces cerevisiae

1999

Wrobel, C.; Schmidt, E.V.; Polymenis, M.

J. Bacteriol.

181

7618-7620

652154

11408489

Species-specific differences in amino acid editing by class II prolyl-tRNA synthetase

2001

Beuning, P.J.; Musier-Forsyth, K.

J. Biol. Chem.

276

30779-30785

652299

12130658

Methanocaldococcus jannaschii prolyl-tRNA synthetase charges tRNA(Pro) with cysteine

2002

Ambrogelly, A.; Ahel, I.; Polycarpo, C.; Bunjun-Srihari, S.; Krett, B.; Jacquin-Becker, C.; Ruan, B.; Kohrer, C.; Stathopoulos, C.; RajBhandary, U.L.; Soll, D.

J. Biol. Chem.

277

34749-34754

653639

11035802

Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase

2000

Chihade, J.W.; Brown, J.R.; Schimmel, P.R.; De Pouplana, L.R.

Proc. Natl. Acad. Sci. USA

97

12153-12157

659068

15901708

Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens

2005

Maillard, A.P.; Biarrotte-Sorin, S.; Villet, R.; Mesnage, S.; Bouhss, A.; Sougakoff, W.; Mayer, C.; Arthur, M.

J. Bacteriol.

187

3833-3838

660520

14962386

Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: Insights into FemABX family substrates recognition

2004

Biarrotte-Sorin, S.; Maillard, A.P.; Delettre, J.; Sougakoff, W.; Arthur, M.; Mayer, C.

Structure

12

257-267

704401

11083873

FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets

2001

Hegde, S.S.; Shrader, T.E.

J. Biol. Chem.

276

6998-7003

705780

19054327

Adaptation of the bacterial membrane to changing environments using aminoacylated phospholipids: MicroCommentary

2009

Roy, H.; Dare, K.; Ibba, M.

Mol. Microbiol.

71

547-550

705781

19087229

Adaptation of Pseudomonas aeruginosa to various conditions includes tRNA-dependent formation of alanyl-phosphatidylglycerol

2009

Klein, S.; Lorenzo, C.; Hoffmann, S.; Walther, J.; Storbeck, S.; Piekarski, T.; Tindall, B.; Wray, V.; Nimtz, M.; Moser, J.

Mol. Microbiol.

71

551-565

712365

-

Kinetic characterization of lipid II-Ala:alanyl-tRNA ligase (MurN) from Streptococcus pneumoniae using semisynthetic aminoacyl-lipid II substrates

2008

De Pascale, G.; Lloyd, A.J.; Schouten, J.A.; Gilbey, a.M.; Roper, D.I.; Dowson, C.G.; Bugg, T.D.H.

J. Biol. Chem.

283

34751-34759

712366

18077448

Characterization of tRNA-dependent peptide bond formation by MurM in the synthesis of Streptococcus pneumoniae peptidoglycan

2008

Lloyd, A.J.; Gilbey, A.M.; Blewett, A.M.; De Pascale, G.; El Zoeiby, A.; Levesque, R.C.; Catherwood, A.C.; Tomasz, A.; Bugg, T.D.H.; Roper, D.I.; Dowson, C.G.

J. Biol. Chem.

283

6402-6417

719738

22267511

Resistance phenotypes mediated by aminoacyl-phosphatidylglycerol synthases

2012

Arendt, W.; Hebecker, S.; Jaeger, S.; Nimtz, M.; Moser, J.

J. Bacteriol.

194

1401-1416

720495

21392131

Alanyl-phosphatidylglycerol synthase: mechanism of substrate recognition during tRNA-dependent lipid modification in Pseudomonas aeruginosa

2011

Hebecker, S.; Arendt, W.; Heinemann, I.U.; Tiefenau, J.H.; Nimtz, M.; Rohde, M.; Soell, D.; Moser, J.

Mol. Microbiol.

80

935-950

736928

23925523

Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla

2013

Mellal, D.; Fonvielle, M.; Santarem, M.; Chemama, M.; Schneider, Y.; Iannazzo, L.; Braud, E.; Arthur, M.; Etheve-Quelquejeu, M.

Org. Biomol. Chem.

11

6161-6169

737171

26261323

Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine

2015

Hebecker, S.; Krausze, J.; Hasenkampf, T.; Schneider, J.; Groenewold, M.; Reichelt, J.; Jahn, D.; Heinz, D.W.; Moser, J.

Proc. Natl. Acad. Sci. USA

112

10691-10696

758682

29574613

Expanding tryptophan-containing cyclodipeptide synthase spectrum by identification of nine members from Streptomyces strains

2018

Liu, J.; Yu, H.; Li, S.M.

Appl. Microbiol. Biotechnol.

102

4435-4444

Links to other databases for L-alanyl-tRNA

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