KEGG   ENZYME: 2.7.11.19Help
Entry
EC 2.7.11.19                Enzyme                                 
Name
phosphorylase kinase;
dephosphophosphorylase kinase;
glycogen phosphorylase kinase;
PHK;
phosphorylase b kinase;
phosphorylase B kinase;
phosphorylase kinase (phosphorylating);
STK17
Class
Transferases;
Transferring phosphorus-containing groups;
Protein-serine/threonine kinases
BRITE hierarchy
Sysname
ATP:phosphorylase-b phosphotransferase
Reaction(IUBMB)
2 ATP + phosphorylase b = 2 ADP + phosphorylase a [RN:R00076]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
phosphorylase b [CPD:C02308]
Product
ADP [CPD:C00008];
phosphorylase a [CPD:C02307]
Comment
Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis---glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b [5]. The gamma subunit of the tetrameric enzyme is the catalytic subunit.
Orthology
K00871  
phosphorylase kinase gamma subunit
Genes
HSA: 
5260(PHKG1) 5261(PHKG2)
PTR: 
741602(PHKG2) 746486(PHKG1)
PPS: 
100983464(PHKG2) 100986631(PHKG1)
GGO: 
101125302(PHKG2) 101134483(PHKG1)
PON: 
100453698(PHKG1) 100455717(PHKG2)
MCC: 
MMU: 
18682(Phkg1) 68961(Phkg2)
RNO: 
100909429 140671(Phkg2) 29353(Phkg1)
CFA: 
489784(PHKG1) 607275(PHKG2)
AML: 
100477667(PHKG1) 100478501(PHKG2)
FCA: 
101081184(PHKG1) 101092572(PHKG2)
BTA: 
512670(PHKG2) 540682(PHKG1)
SSC: 
100310801(PHKG2) 397548(PHGK)
ECB: 
100061404(PHKG1) 100065274(PHKG2)
MDO: 
100012992(PHKG2) 100013442(PHKG1)
SHR: 
100920220(PHKG1) 100927663(PHKG2)
OAA: 
100088260
GGA: 
417543(PHKG1)
MGP: 
100546214(PHKG1)
TGU: 
100221300(PHKG1)
ACS: 
100557980
XLA: 
373780(phkg1) 496328(phkg2)
XTR: 
100145409 448255(phkg1)
DRE: 
393937(phkg2) 554046(phkg1b) 565379(phkg1a)
TRU: 
101077385 101080204
OLA: 
101165598 101167060
BFO: 
BRAFLDRAFT_107074
CIN: 
100182979
SPU: 
582497
DME: 
Dmel_CG1830(PhKgamma)
DPO: 
Dpse_GA14880
DAN: 
Dana_GF20823
DER: 
Dere_GG18438
DPE: 
Dper_GL15144
DSE: 
Dsec_GM13103
DSI: 
Dsim_GD17041
DWI: 
Dwil_GK20076
DYA: 
Dyak_GE15660
DGR: 
Dgri_GH24413
DMO: 
Dmoj_GI16230
DVI: 
Dvir_GJ15921
AGA: 
AgaP_AGAP002647
AAG: 
AaeL_AAEL013755
CQU: 
CpipJ_CPIJ014338
AME: 
550645(PhKgamma)
NVI: 
100117602(NV15452)
TCA: 
655530
API: 
100168501
PHU: 
Phum_PHUM607620
ISC: 
IscW_ISCW015509
CBR: 
CBG15712
BMY: 
Bm1_44555
TSP: 
Tsp_00128
SMM: 
Smp_098840
NVE: 
NEMVE_v1g94804
HMG: 
100207615
AQU: 
100641898
PIC: 
PICST_32412(PAK3)
CAL: 
CaO19.2781
CDU: 
CD36_07120
PTI: 
PHATRDRAFT_14702
 » show all
Taxonomy
Reference
1  [PMID:13315361]
  Authors
KREBS EG, FISCHER EH.
  Title
The phosphorylase b to a converting enzyme of rabbit skeletal muscle.
  Journal
Biochim. Biophys. Acta. 20 (1956) 150-7.
  Organism
Oryctolagus cuniculus
Reference
2  [PMID:13538949]
  Authors
KREBS EG, KENT AB, FISCHER EH.
  Title
The muscle phosphorylase b kinase reaction.
  Journal
J. Biol. Chem. 231 (1958) 73-83.
  Organism
Mus musculus [GN:mmu]
Reference
3  [PMID:13315351]
  Authors
RALL TW, WOSILAIT WD, SUTHERLAND EW.
  Title
The interconversion of phosphorylase a and phosphorylase b from dog heart muscle.
  Journal
Biochim. Biophys. Acta. 20 (1956) 69-76.
  Organism
Canis familiaris [GN:cfa]
Reference
4  [PMID:4029141]
  Authors
Nikolaropoulos S, Sotiroudis TG.
  Title
Phosphorylase kinase from chicken gizzard. Partial purification and characterization.
  Journal
Eur. J. Biochem. 151 (1985) 467-73.
  Organism
Gallus gallus [GN:gga]
Reference
5  [PMID:1931956]
  Authors
Farrar YJ, Carlson GM.
  Title
Kinetic characterization of the calmodulin-activated catalytic subunit of phosphorylase kinase.
  Journal
Biochemistry. 30 (1991) 10274-9.
  Organism
Oryctolagus cuniculus
Reference
6  [PMID:7673209]
  Authors
Dasgupta M, Blumenthal DK.
  Title
Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory.
  Journal
J. Biol. Chem. 270 (1995) 22283-9.
  Organism
Oryctolagus cuniculus
Reference
7  [PMID:9362479]
  Authors
Lowe ED, Noble ME, Skamnaki VT, Oikonomakos NG, Owen DJ, Johnson LN.
  Title
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.
  Journal
EMBO. J. 16 (1997) 6646-58.
  Organism
Oryctolagus cuniculus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9001-88-1
DBGET integrated database retrieval system