M00178
type: Enzyme
rlcp: p397
rlcp: p130
cath: Ribosomal Protein L25; Chain P
cath: Glutamyl-tRNA Synthetase; domain 2
cath: Glutamyl-tRNA Synthetase; domain 3
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/6.1.1.18
csa: 1euy
uniprot: P00962
kegg enzyme: glutamine---tRNA ligase
kegg pathway: Glutamate metabolism
kegg pathway: Aminoacyl-tRNA biosynthesis
kegg cofactor: Magnesium
kegg substrate: ATP
kegg substrate: L-Glutamine
kegg substrate: tRNA(Gln)
kegg product: AMP
kegg product: Pyrophosphate
kegg product: L-Glutaminyl-tRNA(Gln)
pdb: 1euqA01
pdb: 1euyA01
pdb: 1exdA01
pdb: 1gsgP01
pdb: 1gtrA01
pdb: 1gtsA01
pdb: 1nylA01
pdb: 1o0bA01
pdb: 1o0cA01
pdb: 1qrsA01
pdb: 1qrtA01
pdb: 1qruA01
pdb: 1qtqA01
pdb: 1zjwA01
pdb: 1euqA02
pdb: 1euyA02
pdb: 1exdA02
pdb: 1gsgP02
pdb: 1gtrA02
pdb: 1gtsA02
pdb: 1nylA02
pdb: 1o0bA02
pdb: 1o0cA02
pdb: 1qrsA02
pdb: 1qrtA02
pdb: 1qruA02
pdb: 1qtqA02
pdb: 1zjwA02
pdb: 1euqA03
pdb: 1euyA03
pdb: 1exdA03
pdb: 1gsgP03
pdb: 1gtrA03
pdb: 1gtsA03
pdb: 1nylA03
pdb: 1o0bA03
pdb: 1o0cA03
pdb: 1qrsA03
pdb: 1qrtA03
pdb: 1qruA03
pdb: 1qtqA03
pdb: 1zjwA03
pdb: 1euqA04
pdb: 1euyA04
pdb: 1exdA04
pdb: 1gsgP04
pdb: 1gtrA04
pdb: 1gtsA04
pdb: 1nylA04
pdb: 1o0bA04
pdb: 1o0cA04
pdb: 1qrsA04
pdb: 1qrtA04
pdb: 1qruA04
pdb: 1qtqA04
pdb: 1zjwA04
pdb: 1euqA05
pdb: 1euyA05
pdb: 1exdA05
pdb: 1gsgP05

Ribosomal Protein L25; Chain P
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.240.10

Glutamyl-tRNA Synthetase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.1160.10
catalytic domain: index.html

Glutamyl-tRNA Synthetase; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.800.10

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.620
catalytic domain: index.html

Glutamate metabolism
type: KeggPathway
references: KEGG:MAP00251

Aminoacyl-tRNA biosynthesis
type: KeggPathway
references: KEGG:MAP00970

Magnesium
type: KeggCofactor
references: KEGG:C00305
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
references: KEGG:C00002
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Glutamine
type: KeggSubstrate
references: KEGG:C00064
compound type: amino acids
compound type: amide group
references: CHEBI:18050
references: CHEBI:58359
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

tRNA(Gln)
type: KeggSubstrate
references: KEGG:C01640
compound type: nucleic acids

AMP
type: KeggProduct
references: KEGG:C00020
compound type: amine group
compound type: nucleotide
references: CHEBI:16027
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyrophosphate
type: KeggProduct
references: KEGG:C00013
compound type: phosphate group/phosphate ion
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Glutaminyl-tRNA(Gln)
type: KeggProduct
references: KEGG:C02282
compound type: amino acids
compound type: amide group
compound type: nucleic acids

1euqA03
type: Pdb
references: 1euq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1euq
catalytic residue: ARG 260;LYS 270

1euyA03
type: Pdb
references: 1euy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1euy
catalytic residue: ARG 260;LYS 270

1exdA03
type: Pdb
references: 1exd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1exd
catalytic residue: ARG 260;LYS 270

1gsgP03
type: Pdb
references: 1gsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gsg
catalytic residue: ARG 260;LYS 270

1gtrA03
type: Pdb
references: 1gtr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gtr
catalytic residue: ARG 260;LYS 270

1gtsA03
type: Pdb
references: 1gts
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gts
catalytic residue: ARG 260;LYS 270

1nylA03
type: Pdb
references: 1nyl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyl
catalytic residue: ARG 260;LYS 270

1o0bA03
type: Pdb
references: 1o0b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o0b
catalytic residue: ARG 260;LYS 270

1o0cA03
type: Pdb
references: 1o0c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o0c
catalytic residue: ARG 260;LYS 270

1qrsA03
type: Pdb
references: 1qrs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrs
catalytic residue: ARG 260;LYS 270

1qrtA03
type: Pdb
references: 1qrt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrt
catalytic residue: ARG 260;LYS 270

1qruA03
type: Pdb
references: 1qru
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qru
catalytic residue: ARG 260;LYS 270

1qtqA03
type: Pdb
references: 1qtq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qtq
catalytic residue: ARG 260;LYS 270

1zjwA03
type: Pdb
references: 1zjw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zjw
catalytic residue: ARG 260;LYS 270

1euqA05
type: Pdb
references: 1euq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1euq
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1euyA05
type: Pdb
references: 1euy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1euy
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1exdA05
type: Pdb
references: 1exd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1exd
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1gsgP05
type: Pdb
references: 1gsg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gsg
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1gtrA05
type: Pdb
references: 1gtr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gtr
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1gtsA05
type: Pdb
references: 1gts
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gts
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1nylA05
type: Pdb
references: 1nyl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyl
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1o0bA05
type: Pdb
references: 1o0b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o0b
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1o0cA05
type: Pdb
references: 1o0c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o0c
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1qrsA05
type: Pdb
references: 1qrs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrs
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34
comment: mutant D235G

1qrtA05
type: Pdb
references: 1qrt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrt
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34
comment: mutant D235G

1qruA05
type: Pdb
references: 1qru
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qru
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1qtqA05
type: Pdb
references: 1qtq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qtq
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

1zjwA05
type: Pdb
references: 1zjw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zjw
catalytic residue: GLU 34;ASN 36;HIS 43
main chain in catalysis: GLU 34

Analogue
compound: L-Glutamine
pdb: 1o0cA05
ligand het code: GLU

Analogue
compound: tRNA(Gln)
pdb: 1zjwA05
ligand het code: G-C-C-A_976 (chain B:3'-terminus)

Analogue
compound: AMP
pdb: 1exdA05
ligand het code: __A

Analogue
compound: AMP
pdb: 1o0bA05
ligand het code: AMP

Analogue
compound: Pyrophosphate
pdb: 1o0bA05
ligand het code: SO4_1394

Analogue
compound: Pyrophosphate
pdb: 1o0cA05
ligand het code: SO4_1394

Analogue
compound: Pyrophosphate
pdb: 1qtqA05
ligand het code: SO4_1394

Analogue
compound: Pyrophosphate
pdb: 1zjwA05
ligand het code: SO4_1394

IntermediateAnalogue
pdb: 1euqA05
ligand het code: QSI

IntermediateAnalogue
pdb: 1euyA05
ligand het code: QSI

IntermediateAnalogue
pdb: 1qtqA05
ligand het code: QSI

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.13, p.8768-8771

ReferenceForCatalyticMechanism
reference index: 33
reference section: Fig.9, p.446-447
reference step: 2

Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7505222
journal: EMBO J
volume: 12
pages: 5201-8
published year: 1993
authors:
  item: Schwob E
  item: Soll D

Origin of glutaminyl-tRNA synthetase: an example of palimpsest?
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8360919
journal: J Mol Evol
volume: 37
pages: 5-10
published year: 1993
authors:
  item: Di Giulio M

Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8199243
journal: Biochimie
volume: 75
pages: 1083-90
published year: 1993
authors:
  item: Rogers MJ
  item: Weygand-Durasevic I
  item: Schwob E
  item: Sherman JM
  item: Rogers KC
  item: Adachi T
  item: Inokuchi H
  item: Soll D

Overproduction and purification of Escherichia coli tRNA(2Gln) and its use in crystallization of the glutaminyl-tRNA synthetase-tRNA(Gln) complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2459391
journal: J Mol Biol
volume: 202
pages: 121-6
published year: 1988
authors:
  item: Perona JJ
  item: Swanson R
  item: Steitz TA
  item: Soll D

Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2686030
journal: Science
volume: 246
pages: 1152-4
published year: 1989
authors:
  item: Perona JJ
  item: Swanson RN
  item: Rould MA
  item: Steitz TA
  item: Soll D

Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
medline id: 90069584
references: http://www.ncbi.nlm.nih.gov/pubmed/2479982
journal: Science
volume: 246
pages: 1135-42
published year: 1989
authors:
  item: Rould MA
  item: Perona JJ
  item: Soll D
  item: Steitz TA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00962

Structural basis of tRNA discrimination as derived from the high resolution crystal structure of glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2194108
journal: Mol Biol Rep
volume: 14
pages: 213-4
published year: 1990
authors:
  item: Steitz TA
  item: Rould MA
  item: Perona JJ

A fluorescence spectroscopic study of glutaminyl-tRNA synthetase from Escherichia coli and its implications for the enzyme mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1915346
journal: Eur J Biochem
volume: 200
pages: 739-45
published year: 1991
authors:
  item: Bhattacharyya T
  item: Bhattacharyya A
  item: Roy S

Anticodon and acceptor stem nucleotides in tRNA(Gln) are major recognition elements for E. coli glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1857423
journal: Nature
volume: 352
pages: 258-60
published year: 1991
authors:
  item: Jahn M
  item: Rogers MJ
  item: Soll D

Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
medline id: 91312443
references: http://www.ncbi.nlm.nih.gov/pubmed/1857417
journal: Nature
volume: 352
pages: 213-8
published year: 1991
authors:
  item: Rould MA
  item: Perona JJ
  item: Steitz TA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00962

Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2011598
journal: Proc Natl Acad Sci U S A
volume: 88
pages: 2903-7
published year: 1991
authors:
  item: Perona JJ
  item: Rould MA
  item: Steitz TA
  item: Risler JL
  item: Zelwer C
  item: Brunie S

A fluorescence spectroscopic study of substrate-induced conformational changes in glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8369295
journal: Biochemistry
volume: 32
pages: 9268-73
published year: 1993
authors:
  item: Bhattacharyya T
  item: Roy S

Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8364025
journal: Biochemistry
volume: 32
pages: 8758-71
published year: 1993
authors:
  item: Perona JJ
  item: Rould MA
  item: Steitz TA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Relationship between the structure and function of Escherichia coli initiator tRNA.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7515283
journal: Biochimie
volume: 75
pages: 1051-60
published year: 1993
authors:
  item: Dyson MR
  item: Mandal N
  item: RajBhandary UL

Association of tRNA(Gln) acceptor identity with phosphate-sugar backbone interactions observed in the crystal structure of the Escherichia coli glutaminyl-tRNA synthetase-tRNA(Gln) complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8199248
journal: Biochimie
volume: 75
pages: 1125-36
published year: 1993
authors:
  item: McClain WH
  item: Schneider J
  item: Gabriel K

Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7680483
journal: Proc Natl Acad Sci U S A
volume: 90
pages: 2010-4
published year: 1993
authors:
  item: Weygand-Durasevic I
  item: Schwob E
  item: Soll D

Crystal structure of unmodified tRNA(Gln) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8011621
journal: Biochemistry
volume: 33
pages: 7560-7
published year: 1994
authors:
  item: Arnez JG
  item: Steitz TA

Connecting anticodon recognition with the active site of Escherichia coli glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8027995
journal: J Mol Biol
volume: 240
pages: 111-8
published year: 1994
authors:
  item: Weygand-Durasevic I
  item: Rogers MJ
  item: Soll D

Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7506418
journal: Proc Natl Acad Sci U S A
volume: 91
pages: 291-5
published year: 1994
authors:
  item: Rogers MJ
  item: Adachi T
  item: Inokuchi H
  item: Soll D

Substrate selection by aminoacyl-tRNA synthetases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8643392
journal: Nucleic Acids Symp Ser
volume: (33)
pages: 40-2
published year: 1995
authors:
  item: Ibba M
  item: Thomann HU
  item: Hong KW
  item: Sherman JM
  item: Weygand-Durasevic I
  item: Sever S
  item: Stange-Thomann N
  item: Praetorius M
  item: Soll D

Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8942633
journal: Biochemistry
volume: 35
pages: 14725-33
published year: 1996
authors:
  item: Arnez JG
  item: Steitz TA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Aminoacyl-tRNA synthetases optimize both cognate tRNA recognition and discrimination against noncognate tRNAs.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8555233
journal: Biochemistry
volume: 35
pages: 601-7
published year: 1996
authors:
  item: Sherman JM
  item: Soll D

Functional connectivity between tRNA binding domains in glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8601833
journal: J Mol Biol
volume: 256
pages: 818-28
published year: 1996
authors:
  item: Sherman JM
  item: Thomann HU
  item: Soll D

Genetic analysis of functional connectivity between substrate recognition domains of Escherichia coli glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8917315
journal: Mol Gen Genet
volume: 252
pages: 717-22
published year: 1996
authors:
  item: Kitabatake M
  item: Ibba M
  item: Hong KW
  item: Soll D
  item: Inokuchi H

Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8692925
journal: Proc Natl Acad Sci U S A
volume: 93
pages: 6953-8
published year: 1996
authors:
  item: Ibba M
  item: Hong KW
  item: Sherman JM
  item: Sever S
  item: Soll D

Glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9372179
journal: Biol Chem
volume: 378
pages: 1103-17
published year: 1997
authors:
  item: Freist W
  item: Gauss DH
  item: Ibba M
  item: Soll D

RNA base-amino acid interaction strengths derived from structures and sequences.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9185564
journal: Nucleic Acids Res
volume: 25
pages: 2562-5
published year: 1997
authors:
  item: Lustig B
  item: Arora S
  item: Jernigan RL

The terminal adenosine of tRNA(Gln) mediates tRNA-dependent amino acid recognition by glutaminyl-tRNA synthetase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9657697
journal: Biochemistry
volume: 37
pages: 9836-42
published year: 1998
authors:
  item: Liu J
  item: Ibba M
  item: Hong KW
  item: Soll D

The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9799245
journal: EMBO J
volume: 17
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Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex.
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Tertiary core rearrangements in a tight binding transfer RNA aptamer.
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Charging two for the price of one.
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tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase.
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tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase.
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glutaminyl-tRNA synthetase
type: KeggEnzyme

glutaminyl-transfer RNA synthetase
type: KeggEnzyme

glutaminyl-transfer ribonucleate synthetase
type: KeggEnzyme

glutamine-tRNA synthetase
type: KeggEnzyme

glutamine translase
type: KeggEnzyme

glutamate-tRNA ligase
type: KeggEnzyme

glutaminyl ribonucleic acid
type: KeggEnzyme

GlnRS
type: KeggEnzyme