| Entry |
|
|---|
| Name |
myosin ATPase |
|---|
| Class |
Hydrolases;
Acting on acid anhydrides;
Acting on acid anhydrides to facilitate cellular and subcellular
movement
 |
|---|
| Sysname |
ATP phosphohydrolase (actin-translocating) |
|---|
| Reaction(IUBMB) |
ATP + H2O = ADP + phosphate [RN:R00086] |
|---|
| Reaction(KEGG) |
R00086
 |
|---|
| Substrate |
ATP [CPD:C00002];
H2O [CPD:C00001] |
|---|
| Product |
ADP [CPD:C00008];
phosphate [CPD:C00009] |
|---|
| Cofactor |
Calcium [CPD:C00076] |
|---|
| Comment |
Proteins of the contractile apparatus of muscle and nonmuscle cells;
myosin molecule consists of two heavy chains (about 200 kDa) and two
pairs of light chains (15-27 kDa). The head region of the heavy
chain contains actin- and ATP-binding sites. ATP hydrolysis provides
energy for actomyosin contraction. |
|---|
| Pathway |
PATH: ec00230 Purine metabolism |
|---|
| Orthology |
KO: K01553 myosin ATPase |
|---|
| Genes |
DHA: DEHA0G13805g
PIC: PICST_30460(SMC5) PICST_31021(RHC18) PICST_75361(MYO2)
CAL: CaO19.3100
PFA: MAL13P1.148 PF11_0416 PFL1435c
HPA: HPAG1_1080
 |
|---|
| Structures |
PDB: 1W9I 1W9J 1W9K 1W9L |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:8663496]
Rayment I.
The structural basis of the myosin ATPase activity.
J. Biol. Chem. 271 (1996) 15850-3.
Dictyostelium discoideum [GN:ddi] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:8690736]
Hasson T, Mooseker MS.
Vertebrate unconventional myosins.
J. Biol. Chem. 271 (1996) 16431-4.
Homo sapiens [GN:hsa], Mus musculus [GN:mmu], Rattus norvegicus
[GN:rno], Gallus gallus [GN:gga] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:10090768]
Murphy CT, Spudich JA.
The sequence of the myosin 50-20K loop affects Myosin's affinity for
actin throughout the actin-myosin ATPase cycle and its maximum
ATPase activity.
Biochemistry. 38 (1999) 3785-92.
Gallus gallus [GN:gga], Oryctolagus cuniculus, Dictyostelium sp. |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 3.6.4.1
IUBMB Enzyme Nomenclature: 3.6.4.1
ExPASy - ENZYME nomenclature database: 3.6.4.1
BRENDA, the Enzyme Database: 3.6.4.1 |
|---|
