EzCatDB: S00672
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00672
RLCP classification3.103.69910.364 : Transfer
CATH domainDomain 13.40.50.300 : Rossmann foldCatalytic domain
E.C.2.7.1.145

CATH domainRelated DB codes (homologues)
3.40.50.300 : Rossmann foldS00527,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

Enzyme Name
UniProtKBKEGG

Q9XZT6
Protein nameDeoxynucleoside kinaseDeoxynucleoside kinase
Multispecific deoxynucleoside kinase
Ms-dNK
Multisubstrate deoxyribonucleoside kinase
Multifunctional deoxynucleoside kinase
D. melanogaster deoxynucleoside kinase
Dm-dNK
SynonymsEC 2.7.1.145
Deoxyribonucleoside kinase
Dm-dNK
Multispecific deoxynucleoside kinase
RefSeqNP_001262722.1 (Protein)
NM_001275793.1 (DNA/RNA sequence)
NP_524399.1 (Protein)
NM_079675.3 (DNA/RNA sequence)
PfamPF01712 (dNK)
[Graphical view]


UniProtKB:Accession NumberQ9XZT6
Entry nameDNK_DROME
ActivityATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate.
SubunitMonomer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00002C02269C00008C00676
CompoundMagnesiumATP2'-deoxynucleosideADP2'-deoxynucleoside 5'-phosphate
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotidenucleosideamine group,nucleotidenucleotide
ChEBI18420
15422

16761

PubChem888
5957

6022

             
1j90A00UnboundUnboundBound:DCZUnboundUnbound
1j90B00UnboundUnboundBound:DCZUnboundUnbound
1oe0A00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
1oe0B00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
1oe0C00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
1oe0D00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
1ot3A00UnboundUnboundBound:THMUnboundUnbound
1ot3B00UnboundUnboundBound:THMUnboundUnbound
1ot3C00UnboundUnboundBound:THMUnboundUnbound
1ot3D00UnboundUnboundBound:THMUnboundUnbound
1ot3E00UnboundUnboundBound:THMUnboundUnbound
1ot3F00UnboundUnboundBound:THMUnboundUnbound
1ot3G00UnboundUnboundBound:THMUnboundUnbound
1ot3H00UnboundUnboundBound:THMUnboundUnbound
1zm7A00UnboundUnboundUnboundUnboundAnalogue:TTP
1zm7B00UnboundUnboundUnboundUnboundAnalogue:TTP
1zm7C00UnboundUnboundUnboundUnboundAnalogue:TTP
1zm7D00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
1zmxA00UnboundUnboundBound:THMUnboundUnbound
1zmxB00UnboundUnboundBound:THMUnboundUnbound
1zmxC00UnboundUnboundBound:THMUnboundUnbound
1zmxD00UnboundUnboundBound:THMUnboundUnbound
1zmxE00UnboundUnboundBound:THMUnboundUnbound
1zmxF00UnboundUnboundBound:THMUnboundUnbound
1zmxG00UnboundUnboundBound:THMUnboundUnbound
1zmxH00UnboundUnboundBound:THMUnboundUnbound
2jcsA00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
2jcsB00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
2jj8A00UnboundUnboundAnalogue:AAZUnboundUnbound
2jj8B00UnboundUnboundAnalogue:AAZUnboundUnbound
2jj8C00UnboundUnboundAnalogue:AAZUnboundUnbound
2jj8D00UnboundUnboundAnalogue:AAZUnboundUnbound
2vp0A00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
2vp0B00Bound:_MGUnboundUnboundUnboundAnalogue:TTP
2vp2A00UnboundUnboundUnboundUnboundAnalogue:DGT
2vp2B00UnboundUnboundUnboundUnboundAnalogue:DGT
2vp4A00UnboundUnboundUnboundUnboundAnalogue:DCP
2vp4B00UnboundUnboundUnboundUnboundAnalogue:DCP
2vp4C00UnboundUnboundUnboundUnboundAnalogue:DCP
2vp4D00UnboundUnboundUnboundUnboundAnalogue:DCP
2vp5A00UnboundUnboundBound:DCZUnboundUnbound
2vp5B00UnboundUnboundBound:DCZUnboundUnbound
2vp6A00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp6B00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp6C00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp6D00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp6E00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp6F00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp6G00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp6H00UnboundUnboundAnalogue:5FUUnboundUnbound
2vp9A00UnboundUnboundAnalogue:DOCUnboundUnbound
2vp9B00UnboundUnboundAnalogue:DOCUnboundUnbound
2vp9C00UnboundUnboundAnalogue:DOCUnboundUnbound
2vp9D00UnboundUnboundAnalogue:DOCUnboundUnbound
2vp9E00UnboundUnboundAnalogue:DOCUnboundUnbound
2vp9F00UnboundUnboundAnalogue:DOCUnboundUnbound
2vp9G00UnboundUnboundAnalogue:DOCUnboundUnbound
2vp9H00UnboundUnboundAnalogue:DOCUnboundUnbound
2vppA00UnboundUnboundAnalogue:GEOUnboundUnbound
2vppB00UnboundUnboundAnalogue:GEOUnboundUnbound
2vqsA00UnboundUnboundAnalogue:BVDUnboundUnbound
2vqsB00UnboundUnboundAnalogue:BVDUnboundUnbound
2vqsC00UnboundUnboundAnalogue:BVDUnboundUnbound
2vqsD00UnboundUnboundAnalogue:BVDUnboundUnbound

Active-site residues
resource
literature [4], [5], [7], [10]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysiscomment
            
1j90A00LYS 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
1j90B00LYS 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
1oe0A00LYS 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
1oe0B00LYS 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
1oe0C00LYS 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
1oe0D00LYS 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
1ot3A00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1ot3B00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1ot3C00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1ot3D00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1ot3E00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1ot3F00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1ot3G00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1ot3H00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
1zm7A00LYS 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
1zm7B00LYS 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
1zm7C00LYS 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
1zm7D00LYS 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
1zmxA00LYS 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
1zmxB00LYS 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
1zmxC00LYS 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
1zmxD00LYS 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
1zmxE00LYS 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
1zmxF00LYS 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
1zmxG00LYS 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
1zmxH00LYS 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
2jcsA00LYS 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
2jcsB00LYS 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
2jj8A00LYS 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
2jj8B00LYS 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
2jj8C00LYS 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
2jj8D00LYS 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
2vp0A00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
2vp0B00LYS 33;GLU 52;ARG 105;ARG 167;ARG 169
THR 34;GLU 104(Magnesium binding)
GLY 30;SER 31;GLY 32;LYS 33
 
2vp2A00LYS 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
2vp2B00LYS 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
2vp4A00LYS 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
2vp4B00LYS 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
2vp4C00LYS 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
2vp4D00LYS 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
2vp5A00LYS 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
2vp5B00LYS 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
2vp6A00LYS 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
2vp6B00LYS 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
2vp6C00LYS 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
2vp6D00LYS 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
2vp6E00LYS 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
2vp6F00LYS 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
2vp6G00LYS 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
2vp6H00LYS 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
2vp9A00LYS 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
2vp9B00LYS 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
2vp9C00LYS 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
2vp9D00LYS 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
2vp9E00LYS 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
2vp9F00LYS 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
2vp9G00LYS 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
2vp9H00LYS 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
2vppA00LYS 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
2vppB00LYS 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
2vqsA00LYS 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
2vqsB00LYS 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
2vqsC00LYS 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
2vqsD00LYS 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
ReferencesSectionsNo. 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]
CommentsX-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 34-376.
PubMed ID9336833
JournalProtein Sci
Year1997
Volume6
Pages2097-106
AuthorsWild K, Bohner T, Folkers G, Schulz GE
TitleThe structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue.
Related PDB1vtk,2vtk,3vtk
Related UniProtKBP03176
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed ID9715911
JournalProteins
Year1998
Volume32
Pages350-61
AuthorsChampness JN, Bennett MS, Wien F, Visse R, Summers WC, Herdewijn P, de Clerq E, Ostrowski T, Jarvest RL, Sanderson MR
TitleExploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands.
Related PDB1kim
[3]
PubMed ID10692477
JournalJ Biol Chem
Year2000
Volume275
Pages6673-9
AuthorsMunch-Petersen B, Knecht W, Lenz C, Sondergaard L, Piskur J
TitleFunctional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants.
Related UniProtKBQ9XZT6
[4]
PubMed ID11427893
JournalNat Struct Biol
Year2001
Volume8
Pages616-20
AuthorsJohansson K, Ramaswamy S, Ljungcrantz C, Knecht W, Piskur J, Munch-Petersen B, Eriksson S, Eklund H
TitleStructural basis for substrate specificities of cellular deoxyribonucleoside kinases.
Related PDB1j90,1jag
[5]
PubMed ID12363036
JournalCell Mol Life Sci
Year2002
Volume59
Pages1327-46
AuthorsEriksson S, Munch-Petersen B, Johansson K, Eklund H
TitleStructure and function of cellular deoxyribonucleoside kinases.
[6]
PubMed ID11927571
JournalEMBO J
Year2002
Volume21
Pages1873-80
AuthorsKnecht W, Sandrini MP, Johansson K, Eklund H, Munch-Petersen B, Piskur J
TitleA few amino acid substitutions can convert deoxyribonucleoside kinase specificity from pyrimidines to purines.
[7]
PubMed ID12741827
JournalBiochemistry
Year2003
Volume42
Pages5706-12
AuthorsMikkelsen NE, Johansson K, Karlsson A, Knecht W, Andersen G, Piskur J, Munch-Petersen B, Eklund H
TitleStructural basis for feedback inhibition of the deoxyribonucleoside salvage pathway: studies of the Drosophila deoxyribonucleoside kinase.
Related PDB1oe0,1ot3
[8]
PubMed ID12823558
JournalEur J Biochem
Year2003
Volume270
Pages2879-84
AuthorsSolaroli N, Bjerke M, Amiri MH, Johansson M, Karlsson A
TitleActive site mutants of Drosophila melanogaster multisubstrate deoxyribonucleoside kinase.
[9]
PubMed ID16008571
JournalFEBS J
Year2005
Volume272
Pages3733-42
AuthorsWelin M, Skovgaard T, Knecht W, Zhu C, Berenstein D, Munch-Petersen B, Piskur J, Eklund H
TitleStructural basis for the changed substrate specificity of Drosophila melanogaster deoxyribonucleoside kinase mutant N64D.
Related PDB1zm7,1zmx
[10]
PubMed ID17302737
JournalFEBS J
Year2007
Volume274
Pages1542-51
AuthorsEgeblad-Welin L, Sonntag Y, Eklund H, Munch-Petersen B
TitleFunctional 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 PDB2jcs
[11]
PubMed ID18384378
JournalFEBS J
Year2008
Volume275
Pages2151-60
AuthorsMikkelsen NE, Munch-Petersen B, Eklund H
TitleStructural studies of nucleoside analog and feedback inhibitor binding to Drosophila melanogaster multisubstrate deoxyribonucleoside kinase.
Related PDB2jj8,2vp0,2vp2,2vp4,2vp5,2vp6,2vp9,2vqs
[12]
PubMed ID19285960
JournalBiochem Biophys Res Commun
Year2009
Volume382
Pages430-3
AuthorsKnecht W, Mikkelsen NE, Clausen AR, Willer M, Eklund H, Gojkovi? Z, Piskur J
TitleDrosophila melanogaster deoxyribonucleoside kinase activates gemcitabine.
Related PDB2vpp

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.

createdupdated
2009-09-102012-03-02


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.