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: 
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: 
102476302(PHKG1) 102498323(PHKG2)
CFA: 
489784(PHKG1) 607275(PHKG2)
AML: 
100477667(PHKG1) 100478501(PHKG2)
FCA: 
101081184(PHKG1) 101092572(PHKG2)
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)
ECB: 
100061404(PHKG1) 100065274(PHKG2)
MYB: 
102249201(PHKG2) 102254502(PHKG1)
MDO: 
100012992(PHKG2) 100013442(PHKG1)
SHR: 
100920220(PHKG1) 100927663(PHKG2)
OAA: 
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)
PSS: 
102455436(PHKG1)
ACS: 
XLA: 
373780(phkg1) 496328(phkg2)
XTR: 
DRE: 
393937(phkg2) 554046(phkg1b) 565379(phkg1a)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
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: 
PIC: 
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 [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
  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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