DB code: S00672

RLCP classification 3.103.69910.364 : Transfer
CATH domain 3.40.50.300 : Rossmann fold Catalytic domain
E.C. 2.7.1.145
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.300 : Rossmann fold S00527 S00547 S00548 S00550 S00554 S00555 S00671 S00676 S00680 S00682 S00913 S00914 S00301 S00302 S00303 S00304 S00307 S00308 S00305 S00306 S00309 S00310 S00311 M00114 M00199 D00129 D00130 D00540 M00186

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q9XZT6 Deoxynucleoside kinase
EC 2.7.1.145
Deoxyribonucleoside kinase
Dm-dNK
Multispecific deoxynucleoside kinase
NP_001262722.1 (Protein)
NM_001275793.1 (DNA/RNA sequence)
NP_524399.1 (Protein)
NM_079675.3 (DNA/RNA sequence)
PF01712 (dNK)
[Graphical View]

KEGG enzyme name
Deoxynucleoside kinase
Multispecific deoxynucleoside kinase
Ms-dNK
Multisubstrate deoxyribonucleoside kinase
Multifunctional deoxynucleoside kinase
D. melanogaster deoxynucleoside kinase
Dm-dNK

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q9XZT6 DNK_DROME ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate. Monomer.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C02269 C00008 C00676
E.C.
Compound Magnesium ATP 2'-deoxynucleoside ADP 2'-deoxynucleoside 5'-phosphate
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide nucleoside amine group,nucleotide nucleotide
ChEBI 18420
18420
15422
15422
16761
16761
PubChem 888
888
5957
5957
6022
6022
1j90A00 Unbound Unbound Bound:DCZ Unbound Unbound
1j90B00 Unbound Unbound Bound:DCZ Unbound Unbound
1oe0A00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
1oe0B00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
1oe0C00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
1oe0D00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
1ot3A00 Unbound Unbound Bound:THM Unbound Unbound
1ot3B00 Unbound Unbound Bound:THM Unbound Unbound
1ot3C00 Unbound Unbound Bound:THM Unbound Unbound
1ot3D00 Unbound Unbound Bound:THM Unbound Unbound
1ot3E00 Unbound Unbound Bound:THM Unbound Unbound
1ot3F00 Unbound Unbound Bound:THM Unbound Unbound
1ot3G00 Unbound Unbound Bound:THM Unbound Unbound
1ot3H00 Unbound Unbound Bound:THM Unbound Unbound
1zm7A00 Unbound Unbound Unbound Unbound Analogue:TTP
1zm7B00 Unbound Unbound Unbound Unbound Analogue:TTP
1zm7C00 Unbound Unbound Unbound Unbound Analogue:TTP
1zm7D00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
1zmxA00 Unbound Unbound Bound:THM Unbound Unbound
1zmxB00 Unbound Unbound Bound:THM Unbound Unbound
1zmxC00 Unbound Unbound Bound:THM Unbound Unbound
1zmxD00 Unbound Unbound Bound:THM Unbound Unbound
1zmxE00 Unbound Unbound Bound:THM Unbound Unbound
1zmxF00 Unbound Unbound Bound:THM Unbound Unbound
1zmxG00 Unbound Unbound Bound:THM Unbound Unbound
1zmxH00 Unbound Unbound Bound:THM Unbound Unbound
2jcsA00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
2jcsB00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
2jj8A00 Unbound Unbound Analogue:AAZ Unbound Unbound
2jj8B00 Unbound Unbound Analogue:AAZ Unbound Unbound
2jj8C00 Unbound Unbound Analogue:AAZ Unbound Unbound
2jj8D00 Unbound Unbound Analogue:AAZ Unbound Unbound
2vp0A00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
2vp0B00 Bound:_MG Unbound Unbound Unbound Analogue:TTP
2vp2A00 Unbound Unbound Unbound Unbound Analogue:DGT
2vp2B00 Unbound Unbound Unbound Unbound Analogue:DGT
2vp4A00 Unbound Unbound Unbound Unbound Analogue:DCP
2vp4B00 Unbound Unbound Unbound Unbound Analogue:DCP
2vp4C00 Unbound Unbound Unbound Unbound Analogue:DCP
2vp4D00 Unbound Unbound Unbound Unbound Analogue:DCP
2vp5A00 Unbound Unbound Bound:DCZ Unbound Unbound
2vp5B00 Unbound Unbound Bound:DCZ Unbound Unbound
2vp6A00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp6B00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp6C00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp6D00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp6E00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp6F00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp6G00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp6H00 Unbound Unbound Analogue:5FU Unbound Unbound
2vp9A00 Unbound Unbound Analogue:DOC Unbound Unbound
2vp9B00 Unbound Unbound Analogue:DOC Unbound Unbound
2vp9C00 Unbound Unbound Analogue:DOC Unbound Unbound
2vp9D00 Unbound Unbound Analogue:DOC Unbound Unbound
2vp9E00 Unbound Unbound Analogue:DOC Unbound Unbound
2vp9F00 Unbound Unbound Analogue:DOC Unbound Unbound
2vp9G00 Unbound Unbound Analogue:DOC Unbound Unbound
2vp9H00 Unbound Unbound Analogue:DOC Unbound Unbound
2vppA00 Unbound Unbound Analogue:GEO Unbound Unbound
2vppB00 Unbound Unbound Analogue:GEO Unbound Unbound
2vqsA00 Unbound Unbound Analogue:BVD Unbound Unbound
2vqsB00 Unbound Unbound Analogue:BVD Unbound Unbound
2vqsC00 Unbound Unbound Analogue:BVD Unbound Unbound
2vqsD00 Unbound Unbound Analogue:BVD Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [4], [5], [7], [10]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1j90A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
1j90B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
1oe0A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
1oe0B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
1oe0C00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
1oe0D00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
1ot3A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1ot3B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1ot3C00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1ot3D00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1ot3E00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1ot3F00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1ot3G00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1ot3H00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
1zm7A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250
1zm7B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250
1zm7C00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250
1zm7D00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250
1zmxA00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-174
1zmxB00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-174, 195-199
1zmxC00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-173
1zmxD00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-174, 195-199
1zmxE00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-174
1zmxF00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-172, 195-199
1zmxG00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-174
1zmxH00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant N64D, deletion mutant 231-250, invisible 168-173, 195-199
2jcsA00 LYS 33; ;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant E52D, deletion mutant 231-250
2jcsB00 LYS 33; ;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 mutant E52D, deletion mutant 231-250
2jj8A00 LYS 33;GLU 52;ARG 105; ; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 164-173, 194-196
2jj8B00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 168-173, 195-199
2jj8C00 LYS 33;GLU 52;ARG 105; ; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 165-175, 194-199
2jj8D00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 168-173, 195-199
2vp0A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
2vp0B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33
2vp2A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp2B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp4A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp4B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp4C00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp4D00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp5A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp5B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 194-199
2vp6A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp6B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp6C00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp6D00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 194-199
2vp6E00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp6F00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp6G00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp6H00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp9A00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp9B00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp9C00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250
2vp9D00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 194-199
2vp9E00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp9F00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp9G00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vp9H00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 195-199
2vppA00 LYS 33;GLU 52;ARG 105;ARG 167;ARG 169 THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 198-200
2vppB00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 168-169, 198-200
2vqsA00 LYS 33;GLU 52;ARG 105; ; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 164-175, 194-196
2vqsB00 LYS 33;GLU 52;ARG 105;ARG 167; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 168-173, 194-196
2vqsC00 LYS 33;GLU 52;ARG 105; ; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 167-175, 194-195
2vqsD00 LYS 33;GLU 52;ARG 105; ; THR 34;GLU 104(Magnesium binding) GLY 30;SER 31;GLY 32;LYS 33 deletion mutant 231-250, invisible 165-173, 195-199

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.617-618
[5]
Fig.7, p.1338-1339
[7]
p.5710, p.5711
[10]
p.1544-1548

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 34-376.
Medline ID
PubMed ID 9336833
Journal Protein Sci
Year 1997
Volume 6
Pages 2097-106
Authors Wild K, Bohner T, Folkers G, Schulz GE
Title The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue.
Related PDB 1vtk 2vtk 3vtk
Related UniProtKB P03176
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID
PubMed ID 9715911
Journal Proteins
Year 1998
Volume 32
Pages 350-61
Authors Champness JN, Bennett MS, Wien F, Visse R, Summers WC, Herdewijn P, de Clerq E, Ostrowski T, Jarvest RL, Sanderson MR
Title Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands.
Related PDB 1kim
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10692477
Journal J Biol Chem
Year 2000
Volume 275
Pages 6673-9
Authors Munch-Petersen B, Knecht W, Lenz C, Sondergaard L, Piskur J
Title Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants.
Related PDB
Related UniProtKB Q9XZT6
[4]
Resource
Comments
Medline ID
PubMed ID 11427893
Journal Nat Struct Biol
Year 2001
Volume 8
Pages 616-20
Authors Johansson K, Ramaswamy S, Ljungcrantz C, Knecht W, Piskur J, Munch-Petersen B, Eriksson S, Eklund H
Title Structural basis for substrate specificities of cellular deoxyribonucleoside kinases.
Related PDB 1j90 1jag
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 12363036
Journal Cell Mol Life Sci
Year 2002
Volume 59
Pages 1327-46
Authors Eriksson S, Munch-Petersen B, Johansson K, Eklund H
Title Structure and function of cellular deoxyribonucleoside kinases.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11927571
Journal EMBO J
Year 2002
Volume 21
Pages 1873-80
Authors Knecht W, Sandrini MP, Johansson K, Eklund H, Munch-Petersen B, Piskur J
Title A few amino acid substitutions can convert deoxyribonucleoside kinase specificity from pyrimidines to purines.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12741827
Journal Biochemistry
Year 2003
Volume 42
Pages 5706-12
Authors Mikkelsen NE, Johansson K, Karlsson A, Knecht W, Andersen G, Piskur J, Munch-Petersen B, Eklund H
Title Structural basis for feedback inhibition of the deoxyribonucleoside salvage pathway: studies of the Drosophila deoxyribonucleoside kinase.
Related PDB 1oe0 1ot3
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12823558
Journal Eur J Biochem
Year 2003
Volume 270
Pages 2879-84
Authors Solaroli N, Bjerke M, Amiri MH, Johansson M, Karlsson A
Title Active site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 16008571
Journal FEBS J
Year 2005
Volume 272
Pages 3733-42
Authors Welin M, Skovgaard T, Knecht W, Zhu C, Berenstein D, Munch-Petersen B, Piskur J, Eklund H
Title Structural basis for the changed substrate specificity of Drosophila melanogaster deoxyribonucleoside kinase mutant N64D.
Related PDB 1zm7 1zmx
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 17302737
Journal FEBS J
Year 2007
Volume 274
Pages 1542-51
Authors Egeblad-Welin L, Sonntag Y, Eklund H, Munch-Petersen B
Title Functional studies of active-site mutants from Drosophila melanogaster deoxyribonucleoside kinase. Investigations of the putative catalytic glutamate-arginine pair and of residues responsible for substrate specificity.
Related PDB 2jcs
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 18384378
Journal FEBS J
Year 2008
Volume 275
Pages 2151-60
Authors Mikkelsen NE, Munch-Petersen B, Eklund H
Title Structural studies of nucleoside analog and feedback inhibitor binding to Drosophila melanogaster multisubstrate deoxyribonucleoside kinase.
Related PDB 2jj8 2vp0 2vp2 2vp4 2vp5 2vp6 2vp9 2vqs
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 19285960
Journal Biochem Biophys Res Commun
Year 2009
Volume 382
Pages 430-3
Authors Knecht W, Mikkelsen NE, Clausen AR, Willer M, Eklund H, Gojkovi? Z, Piskur J
Title Drosophila melanogaster deoxyribonucleoside kinase activates gemcitabine.
Related PDB 2vpp
Related UniProtKB

Comments
This enzyme is closely related to deoxycytidine kinase (EC 2.7.1.74; S00682 in EzCatDB), and share a similar active site with the homologous enzyme. Thus, the catalytic mechanism of this enzyme seems to be the same as that of the homologous enzyme, deoxycytidine kinase.
According to the literature [5] and [7], dTTP is a strong competitive inhibitor for this enzyme, and can bind with the base at the deoxynucleoside-binding site. Although Glu52 acts as a general base to activate 5'-OH of the deoxynucleoside, it would shift from the position, to coordinate magnesium ion, along with Thr34 and Glu104 in the dTTP inhibitor complex.

Created Updated
2009-09-10 2012-03-02