Sequence of KARG_LIMPO
EC Number:2.7.3.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
Other sequences found for EC No. 2.7.3.3
General information:
Sequence
0 MVDQATLDKL EAGFKKLQEA SDCKSLLKKH LTKDVFDSIK NKKTGMGATL LDVIQSGVEN
60 LDSGVGIYAP DAESYRTFGP LFDPIIDDYH GGFKLTDKHP PKEWGDINTL VDLDPGGQFI
120 ISTRVRCGRS LQGYPFNPCL TAEQYKEMEE KVSSTLSSME DELKGTYYPL TGMSKATQQQ
180 LIDDHFLFKE GDRFLQTANA CRYWPTGRGI FHNDAKTFLV WVNEEDHLRI ISMQKGGDLK
240 TVYKRLVTAV DNIESKLPFS HDDRFGFLTF CPTNLGTTMR ASVHIQLPKL AKDRKVLEDI
300 ASKFNLQVRG TRGEHTESEG GVYDISNKRR LGLTEYQAVR EMQDGILEMI KMEKAAA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
309228
Strong S.J.,Ellington W.R.
Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues.
Biochim. Biophys. Acta
1246
197-200
1995
309229
Zhou G.,Somasundaram T.,Blanc E.,Parthasarathy G.,Ellington W.R.,Chapman M.S.
Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions.
Proc. Natl. Acad. Sci. U.S.A.
95
8449-8454
1998
309230
Yousef M.S.,Fabiola F.,Gattis J.L.,Somasundaram T.,Chapman M.S.
Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.
Acta Crystallogr. D
58
2009-2017
2002
309231
Pruett P.S.,Azzi A.,Clark S.A.,Yousef M.S.,Gattis J.L.,Somasundaram T.,Ellington W.R.,Chapman M.S.
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
J. Biol. Chem.
278
26952-26957
2003
309232
Azzi A.,Clark S.A.,Ellington W.R.,Chapman M.S.
The role of phosphagen specificity loops in arginine kinase.
Protein Sci.
13
575-585
2004
309233
Gattis J.L.,Ruben E.,Fenley M.O.,Ellington W.R.,Chapman M.S.
The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants.
Biochemistry
43
8680-8689
2004
