Enzyme

Download
EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.234
Description:N(6)-L-threonylcarbamoyladenine synthase.
Alternative Name: T6A synthase.
Cath: 1.10.510.10; 3.30.200.20; 3.30.420.40;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.234
BRENDA Enzyme Link: BRENDA 2.3.1.234
KEGG Enzyme Link: KEGG2.3.1.234
BioCyc Enzyme Link: BioCyc 2.3.1.234
ExPASy Enzyme Link: ExPASy2.3.1.234
EC2PDB Enzyme Link: EC2PDB 2.3.1.234
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.234
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.234
IntEnz Enzyme Link: IntEnz 2.3.1.234
MEDLINE Enzyme Link: MEDLINE 2.3.1.234
MSA:

2.3.1.234;

Phylogenetic Tree:

2.3.1.234;

Uniprot:
M-CSA:
RHEA:37059 adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[NH2;+0:7]>>[*:6]-[NH;+0:7]-[C;H0;+0:2](-[*:1])=[*:3].[*:5]-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya.Perrochia L, Crozat E, Hecker A, Zhang W, Bareille J, Collinet B, van Tilbeurgh H, Forterre P, Basta T2013 Feb 123258706
Mechanism of N6-threonylcarbamoyladenonsine (t(6)A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP.Lauhon CT2012 Nov 623072323