KEGG   ENZYME: 2.7.11.18Help
Entry
EC 2.7.11.18                Enzyme                                 

Name
myosin-light-chain kinase;
[myosin-light-chain] kinase;
ATP:myosin-light-chain O-phosphotransferase;
calcium/calmodulin-dependent myosin light chain kinase;
MLCK;
MLCKase;
myosin kinase;
myosin light chain kinase;
myosin light chain protein kinase;
myosin light-chain kinase (phosphorylating);
smooth-muscle-myosin-light-chain kinase;
STK18
Class
Transferases;
Transferring phosphorus-containing groups;
Protein-serine/threonine kinases
BRITE hierarchy
Sysname
ATP:[myosin light chain] O-phosphotransferase
Reaction(IUBMB)
ATP + [myosin light chain] = ADP + [myosin light chain] phosphate [RN:R03150]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
myosin light chain [CPD:C01003]
Product
ADP [CPD:C00008];
myosin light chain phosphate [CPD:C03875]
Comment
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.
History
EC 2.7.11.18 created 1986 as EC 2.7.1.117, transferred 2005 to EC 2.7.11.18
Orthology
K00907  
myosin-light-chain kinase
Genes
HSA: 
340156(MYLK4) 4638(MYLK) 85366(MYLK2) 91807(MYLK3)
PTR: 
101057233(MYLK) 460640(MYLK) 465143(MYLK3) 471840(MYLK4) 742591(MYLK2)
PPS: 
100974667(MYLK3) 100978891(MYLK2) 100979422(MYLK) 100995666(MYLK4)
GGO: 
101142619(MYLK3) 101143745(MYLK2) 101151517(MYLK) 101151667(MYLK4)
PON: 
100171951(MYLK3) 100444714(MYLK4) 100452913(MYLK) 100453783(MYLK2)
MCC: 
707361(MYLK4) 712830 715422(MYLK) 716132(MYLK3)
MCF: 
102122026(MYLK4) 102130711(MYLK) 102132754(MYLK3) 102145766(MYLK2)
MMU: 
107589(Mylk) 213435(Mylk3) 228785(Mylk2) 238564(Mylk4)
RNO: 
100911165(Mylk4) 117558(Mylk2) 288057(Mylk) 291926(Mylk3)
CGE: 
100755963(Mylk2) 100756400(Mylk4) 100758406(Mylk) 100766446(Mylk3)
HGL: 
101697894(Mylk3) 101701713(Mylk4) 101704236(Mylk) 101712444(Mylk2)
TUP: 
102468205(MYLK3) 102476504(MYLK) 102489117(MYLK2) 102498032(MYLK4)
CFA: 
475345(MYLK3) 477187(MYLK2) 488012(MYLK) 488190(MYLK4)
AML: 
FCA: 
101088408(MYLK4) 101091744(MYLK3) 101095813(MYLK2) 494213
PTG: 
102951994(MYLK2) 102962607(MYLK3) 102968305(MYLK4) 102972928(MYLK)
BTA: 
338037(MYLK) 518025(MYLK4) 526379(MYLK3) 533378(MYLK2)
BOM: 
102264349(MYLK4) 102269080(MYLK) 102275601(MYLK3) 102276600(MYLK2)
PHD: 
102331525(MYLK2) 102337475(MYLK) 102337545(MYLK3)
CHX: 
102181454(MYLK4) 102181980(MYLK3) 102182147(MYLK2) 102190641(MYLK)
SSC: 
100157526(MYLK4) 100524288(MYLK2) 396848(MYLK)
CFR: 
102505869(MYLK2) 102511426(MYLK3) 102515628(MYLK4) 102518144(MYLK)
BACU: 
103005866(MYLK3) 103008421(MYLK) 103017148(MYLK2) 103020477(MYLK4)
LVE: 
103077707(MYLK4) 103079981(MYLK2) 103083551(MYLK3) 103090456(MYLK)
ECB: 
100050092(MYLK4) 100053698(MYLK2) 100056559(MYLK3) 100070482(MYLK)
MYB: 
MYD: 
102755283(MYLK2) 102759237(MYLK) 102765242(MYLK4) 102769513(MYLK3)
PALE: 
102878549(MYLK3) 102890778(MYLK) 102891799(MYLK2) 102894361(MYLK4)
MDO: 
100010869(MYLK2) 100015876(MYLK3) 100019648(MYLK) 100021377(MYLK4)
SHR: 
100915288(MYLK2) 100925131(MYLK3) 100930073(MYLK)
OAA: 
GGA: 
396356(MYLK2) 396445(MYLK) 415748(MYLK3) 420893(MYLK4) 428278
MGP: 
TGU: 
FAB: 
PHI: 
102101059 102104582(MYLK2) 102106790(MYLK) 102111091(MYLK4) 102112254(MYLK3)
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
102369318(MYLK2) 102371849(MYLK3) 102381743(MYLK) 102384108(MYLK4) 102387857
AMJ: 
102557905 102560523(MYLK2) 102561520(MYLK) 102568638(MYLK3) 102574082(MYLK4)
PSS: 
102448460(MYLK4) 102458914(MYLK3) 102461334(MYLK2) 102461616(MYLK)
CMY: 
ACS: 
PBI: 
XTR: 
DRE: 
100003770 449707(mylk4b) 492576(mylkb) 558685(mlck2) 561635(mylk3) 566845 569510(mylka)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
413190(GB14586)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_ZC373.4(ZC373.4)
CBR: 
BMY: 
LOA: 
NVE: 
TAD: 
PFA: 
PFH: 
PYO: 
PBE: 
PKN: 
PVX: 
 » show all
Taxonomy
Reference
1  [PMID:6894756]
  Authors
Adelstein RS, Klee CB.
  Title
Purification and characterization of smooth muscle myosin light chain kinase.
  Journal
J. Biol. Chem. 256 (1981) 7501-9.
  Organism
Meleagris gallopavo
Reference
2  [PMID:156362]
  Authors
Hathaway DR, Adelstein RS.
  Title
Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 1653-7.
  Organism
Homo sapiens
Reference
3  [PMID:4853304]
  Authors
Pires E, Perry SV, Thomas MA.
  Title
Myosin light-chain kinase, a new enzyme from striated muscle.
  Journal
FEBS. Lett. 41 (1974) 292-6.
  Organism
Oryctolagus cuniculus
Reference
4  [PMID:3881420]
  Authors
Nunnally MH, Rybicki SB, Stull JT.
  Title
Characterization of chicken skeletal muscle myosin light chain kinase. Evidence for muscle-specific isozymes.
  Journal
J. Biol. Chem. 260 (1985) 1020-6.
  Organism
Gallus gallus
Reference
5  [PMID:3897230]
  Authors
Edelman AM, Takio K, Blumenthal DK, Hansen RS, Walsh KA, Titani K, Krebs EG.
  Title
Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase.
  Journal
J. Biol. Chem. 260 (1985) 11275-85.
  Organism
Oryctolagus cuniculus
Reference
6  [PMID:12390014]
  Authors
Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M.
  Title
Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR.
  Journal
Biochemistry. 41 (2002) 12899-906.
  Organism
Gallus gallus
Reference
7  [PMID:10231558]
  Authors
Sobieszek A.
  Title
Enzyme kinetic characterization of the smooth muscle myosin phosphorylating system: activation by calcium and calmodulin and possible inhibitory mechanisms of antagonists.
  Journal
Biochim. Biophys. Acta. 1450 (1999) 77-91.
  Organism
Meleagris gallopavo
Reference
8  [PMID:9054394]
  Authors
Sobieszek A, Borkowski J, Babiychuk VS.
  Title
Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex.
  Journal
J. Biol. Chem. 272 (1997) 7034-41.
  Organism
Meleagris gallopavo
Reference
9  [PMID:10098974]
  Authors
Fujita K, Ye LH, Sato M, Okagaki T, Nagamachi Y, Kohama K.
  Title
Myosin light chain kinase from skeletal muscle regulates an ATP-dependent interaction between actin and myosin by binding to actin.
  Journal
Mol. Cell. Biochem. 190 (1999) 85-90.
  Organism
Gallus gallus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
51845-53-5

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