Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.297
Description:Peptide chain release factor N(5)-glutamine methyltransferase.
Alternative Name: N(5)-glutamine S-adenosyl-L-methionine dependent methyltransferase.
N(5)-glutamine MTase.
Cath: 1.10.8.10; 3.40.50.150;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.297
BRENDA Enzyme Link: BRENDA 2.1.1.297
KEGG Enzyme Link: KEGG2.1.1.297
BioCyc Enzyme Link: BioCyc 2.1.1.297
ExPASy Enzyme Link: ExPASy2.1.1.297
EC2PDB Enzyme Link: EC2PDB 2.1.1.297
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.297
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.297
IntEnz Enzyme Link: IntEnz 2.1.1.297
MEDLINE Enzyme Link: MEDLINE 2.1.1.297
MSA:

2.1.1.297;

Phylogenetic Tree:

2.1.1.297;

Uniprot:
M-CSA:
RHEA:42896 L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[NH;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase.Yang Z, Shipman L, Zhang M, Anton BP, Roberts RJ, Cheng X2004 Jul 1615223314
X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase.Yoon HJ, Kang KY, Ahn HJ, Shim SM, Ha JY, Lee SK, Mikami B, Suh SW2003 Oct 3114651272
Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase.Schubert HL, Phillips JD, Hill CP2003 May 2012741815
The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors.Heurgué-Hamard V, Champ S, Engström A, Ehrenberg M, Buckingham RH2002 Feb 1511847124