EzCatDB: D00127
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DB codeD00127
CATH domainDomain 11.10.135.10 : Transferase Creatine Kinase; Chain A, domain 1
Domain 23.30.590.10 : Creatine Kinase; Chain A, domain 2Catalytic domain
E.C.2.7.3.3
CSA1bg0
MACiEM0086


Enzyme Name
UniProtKBKEGG

P51541
Protein nameArginine kinasearginine kinase
arginine phosphokinase
adenosine 5'-triphosphate: L-arginine phosphotransferase
adenosine 5'-triphosphate-arginine phosphotransferase
ATP:L-arginine N-phosphotransferasel ATP:L-arginineomega-N-phosphotransferase
SynonymsAK
EC 2.7.3.3
PfamPF00217 (ATP-gua_Ptrans)
PF02807 (ATP-gua_PtransN)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00330Arginine and proline metabolism

UniProtKB:Accession NumberP51541
Entry nameKARG_LIMPO
ActivityATP + L-arginine = ADP + N(omega)-phospho-L- arginine.
SubunitMonomer.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00305C00002C00062C00008C05945
CompoundMagnesiumATPL-ArginineADPN-Phospho-L-arginine
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotideamino acids,amine group,imine group,lipidamine group,nucleotideamino acids,amine group,imine group,lipid,phosphate group/phosphate ion
ChEBI18420
15422
16467
16761
18412

PubChem888
5957
6322
28782
6022
92150

              
1bg0A01UnboundUnboundUnboundUnboundUnboundUnbound
1m80A01UnboundUnboundUnboundUnboundUnboundUnbound
1m80B01UnboundUnboundUnboundUnboundUnboundUnbound
1m15A01UnboundUnboundUnboundUnboundUnboundUnbound
1p50A01UnboundUnboundUnboundUnboundUnboundUnbound
1p52A01UnboundUnboundUnboundUnboundUnboundUnbound
1bg0A02Bound:_MGUnboundAnalogue:DARBound:ADPUnboundTransition-state-analogue:NO3 401
1m80A02UnboundUnboundUnboundUnboundUnboundUnbound
1m80B02UnboundUnboundUnboundUnboundUnboundUnbound
1m15A02Bound:_MGUnboundBound:ARGBound:ADPUnboundTransition-state-analogue:NO3 405
1p50A02Bound:_MGUnboundBound:ARGBound:ADPUnboundTransition-state-analogue:NO3
1p52A02Bound:_MGUnboundAnalogue:DARBound:ADPUnboundTransition-state-analogue:NO3 401

Active-site residues
resource
Swiss-prot;P51541
pdbCatalytic residues
         
1bg0A01 
1m80A01 
1m80B01 
1m15A01 
1p50A01 
1p52A01 
1bg0A02CYS 271
1m80A02CYS 271
1m80B02CYS 271
1m15A02CYS 271
1p50A02CYS 271
1p52A02CYS 271

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Fig.3, p.8451-8453
[10]p.26956-26957

references
[1]
PubMed ID7819288
JournalBiochim Biophys Acta
Year1995
Volume1246
Pages197-200
AuthorsStrong SJ, Ellington WR
TitleIsolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues.
[2]
PubMed ID9359868
JournalBiochem J
Year1997
Volume328
Pages301-6
AuthorsSuzuki T, Kawasaki Y, Furukohri T
TitleEvolution of phosphagen kinase. Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus.
[3]
PubMed ID9675202
JournalBiophys J
Year1998
Volume75
Pages1016-23
AuthorsForstner M, Kriechbaum M, Laggner P, Wallimann T
TitleStructural changes of creatine kinase upon substrate binding.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS)
Medline ID98337935
PubMed ID9671698
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages8449-54
AuthorsZhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS
TitleTransition state structure of arginine kinase: implications for catalysis of bimolecular reactions.
Related PDB1bg0
Related UniProtKBP51541
[5]
PubMed ID10089314
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages835-45
AuthorsZhou G, Somasundaram T, Blanc E, Chen Z, Chapman MS
TitleCritical initial real-space refinement in the structure determination of arginine kinase.
[6]
PubMed ID10461938
JournalJ Parasitol
Year1999
Volume85
Pages603-7
AuthorsPlatzer EG, Wang W, Thompson SN, Borchardt DB
TitleArginine kinase and phosphoarginine, a functional phosphagen, in the rhabditoid nematode steinernema carpocapsae.
[7]
PubMed ID10811656
JournalJ Biol Chem
Year2000
Volume275
Pages23884-90
AuthorsSuzuki T, Fukuta H, Nagato H, Umekawa M
TitleArginine kinase from Nautilus pompilius, a living fossil. Site-directed mutagenesis studies on the role of amino acid residues in the Guanidino specificity region.
[8]
PubMed ID12454458
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages2009-17
AuthorsYousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS
TitleRefinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.
Related PDB1m15
[9]
PubMed ID12493833
JournalProtein Sci
Year2003
Volume12
Pages103-11
AuthorsYousef MS, Clark SA, Pruett PK, Somasundaram T, Ellington WR, Chapman MS
TitleInduced fit in guanidino kinases--comparison of substrate-free and transition state analog structures of arginine kinase.
Related PDB1m80
[10]
PubMed ID12732621
JournalJ Biol Chem
Year2003
Volume278
Pages26952-7
AuthorsPruett PS, Azzi A, Clark SA, Yousef MS, Gattis JL, Somasundaram T, Ellington WR, Chapman MS
TitleThe putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
Related PDB1p50,1p52


createdupdated
2004-03-182009-02-26


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