Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.20
Description:Adenosine kinase.
Prosite: PDOC00504;
PDB:
PDBScop
Cath: 3.30.1110.10; 3.40.1190.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.20
BRENDA Enzyme Link: BRENDA 2.7.1.20
KEGG Enzyme Link: KEGG2.7.1.20
BioCyc Enzyme Link: BioCyc 2.7.1.20
ExPASy Enzyme Link: ExPASy2.7.1.20
EC2PDB Enzyme Link: EC2PDB 2.7.1.20
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.20
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.20
IntEnz Enzyme Link: IntEnz 2.7.1.20
MEDLINE Enzyme Link: MEDLINE 2.7.1.20
MSA:

2.7.1.20;

Phylogenetic Tree:

2.7.1.20;

Uniprot:
M-CSA:
RHEA:20824 adenosine + ATP = ADP + AMP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structure of human adenosine kinase at 1.5 A resolution.Mathews II, Erion MD, Ealick SE1998 Nov 109843365
Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside.KORNBERG A, PRICER WE Jr1951 Dec14907737
The enzymatic synthesis of adenylic acid; adenosinekinase.CAPUTTO R1951 Apr14832298
Identification and characterization of a unique adenosine kinase from Mycobacterium tuberculosis.Long MC, Escuyer V, Parker WB2003 Nov14594827