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.
History
EC 2.7.11.19 created 1961 as EC 2.7.1.38, transferred 2005 to EC 2.7.11.19
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: 
MCF: 
102125953(PHKG1) 102128006(PHKG2)
MMU: 
18682(Phkg1) 68961(Phkg2)
RNO: 
100909429 140671(Phkg2) 29353(Phkg1)
CGE: 
100750910(Phkg2) 100754334(Phkg1)
HGL: 
101700591(Phkg2) 101707775(Phkg1)
TUP: 
CFA: 
489784(PHKG1) 607275(PHKG2)
AML: 
100477667(PHKG1) 100478501(PHKG2)
FCA: 
101081184(PHKG1) 101092572(PHKG2)
PTG: 
102958678(PHKG2) 102965580(PHKG1)
BTA: 
512670(PHKG2) 540682(PHKG1)
BOM: 
102266225(PHKG1) 102279229(PHKG2)
PHD: 
102338518(PHKG2) 102339551(PHKG1)
CHX: 
100861337(PHKG2) 102185139(PHKG1)
SSC: 
100310801(PHKG2) 397548(PHGK)
CFR: 
102509900(PHKG1) 102517940(PHKG2)
BACU: 
103011969(PHKG1) 103020540(PHKG2)
LVE: 
103069260(PHKG1) 103082932(PHKG2)
ECB: 
100061404(PHKG1) 100065274(PHKG2)
MYB: 
102249201(PHKG2) 102254502(PHKG1)
MYD: 
102751284(PHKG2) 102760309(PHKG1)
PALE: 
102879938(PHKG1) 102882222(PHKG2)
MDO: 
100012992(PHKG2) 100013442(PHKG1)
SHR: 
100920220(PHKG1) 100927663(PHKG2)
OAA: 
100088260(PHKG1)
GGA: 
417543(PHKG1)
MGP: 
100546214(PHKG1)
TGU: 
100221300(PHKG1)
FAB: 
101811164(PHKG1)
PHI: 
102104524(PHKG1)
APLA: 
101793068(PHKG1)
FPG: 
101920077(PHKG1)
FCH: 
102054686(PHKG1)
CLV: 
102085380(PHKG1)
ASN: 
102372756(PHKG1) 102380957(PHKG2)
AMJ: 
102572090(PHKG2) 102574725(PHKG1)
PSS: 
102445349(PHKG2) 102455436(PHKG1)
CMY: 
102934958(PHKG2) 102939493(PHKG1)
ACS: 
PBI: 
103061914(PHKG2) 103065315(PHKG1)
XLA: 
373780(phkg1) 496328(phkg2)
XTR: 
DRE: 
393937(phkg2) 554046(phkg1b) 565379(phkg1a)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
103188445(phkg1)
BFO: 
CIN: 
SPU: 
DME: 
Dmel_CG1830(PhKgamma)
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
550645(PhKgamma)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CBR: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
AQU: 
CSL: 
PIC: 
SPAA: 
CAL: 
CDU: 
PTI: 
 » 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
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
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
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
  Sequence
[up:P00518]
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
  Sequence
[up:P00518]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9001-88-1

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