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)
NLE: 100588039(PHKG2) 100594015(PHKG1)
MCC: 100423096(PHKG2) 703091(PHKG1)
MCF: 102125953(PHKG1) 102128006(PHKG2)
CSAB: 103226033(PHKG1) 103231030 103231924(PHKG2)
RRO: 104661547(PHKG2) 104675874(PHKG1)
RBB: 108526509(PHKG1) 108530886(PHKG2)
CJC: 100412760(PHKG2) 100414478(PHKG1)
SBQ: 101045885(PHKG2) 101048522(PHKG1)
MMU: 18682(Phkg1) 68961(Phkg2)
RNO: 140671(Phkg2) 29353(Phkg1)
CGE: 100750910(Phkg2) 100754334(Phkg1)
NGI: 103726346(Phkg2) 103738953(Phkg1)
HGL: 101700591(Phkg2) 101707775(Phkg1)
CCAN: 109677759(Phkg1) 109682498(Phkg2)
OCU: 100009297(PHKG1) 100355661(PHKG2)
TUP: 102476302(PHKG1) 102480103(PHKG2) 102498323
CFA: 489784(PHKG1) 607275(PHKG2)
AML: 100477667(PHKG1) 100478501(PHKG2)
UMR: 103657874(PHKG2) 103670188(PHKG1)
ORO: 101366392(PHKG1) 101373618(PHKG2)
FCA: 101081184(PHKG1) 101092572(PHKG2)
PTG: 102958678(PHKG2) 102965580(PHKG1)
AJU: 106972855(PHKG1) 106979102(PHKG2)
BTA: 512670(PHKG2) 540682(PHKG1)
BOM: 102266225(PHKG1) 102279229(PHKG2)
BIU: 109578248(PHKG1) 109578294(PHKG2)
PHD: 102338518(PHKG2) 102339551(PHKG1)
CHX: 100861337(PHKG2) 102185139(PHKG1)
OAS: 100217403(PHKG2) 101109323(PHKG1)
SSC: 100310801(PHKG2) 397548(PHKG1)
CFR: 102509900(PHKG1) 102517940(PHKG2)
CDK: 105089705(PHKG1) 105102728(PHKG2)
BACU: 103011969(PHKG1) 103020540(PHKG2)
LVE: 103069260(PHKG1) 103082932(PHKG2)
OOR: 101270202(PHKG1) 101281573(PHKG2)
ECB: 100061404(PHKG1) 100065274(PHKG2)
EPZ: 103547228(PHKG2) 103566047(PHKG1)
EAI: 106831860(PHKG1) 106831907(PHKG2)
MYB: 102249201(PHKG2) 102254502(PHKG1)
MYD: 102751284(PHKG2) 102760309(PHKG1)
HAI: 109374179(PHKG2) 109376279(PHKG1)
RSS: 109437800(PHKG2) 109438915(PHKG1)
PALE: 102879938(PHKG1) 102882222(PHKG2)
LAV: 100660711(PHKG2) 100663820(PHKG1)
MDO: 100012992(PHKG2) 100013442(PHKG1)
SHR: 100920220(PHKG1) 100927663(PHKG2)
OAA: 100088260(PHKG1) 100093441(PHKG2)
GGA: 417543(PHKG1)
MGP: 100546214(PHKG1)
CJO: 107322445(PHKG1)
APLA: 101793068(PHKG1)
ACYG: 106041427(PHKG1)
TGU: 100221300(PHKG1)
GFR: 102038175(PHKG1)
FAB: 101811164(PHKG1)
PHI: 102104524(PHKG1)
PMAJ: 107212749(PHKG1)
CCAE: 111937725(PHKG1)
CCW: 104691086(PHKG1)
FPG: 101920077(PHKG1)
FCH: 102054686(PHKG1)
CLV: 102085380(PHKG1)
EGZ: 104131918(PHKG1)
ASN: 102372756(PHKG1) 102380957(PHKG2)
AMJ: 102572090(PHKG2) 102574725(PHKG1)
PSS: 102445349(PHKG2) 102455436(PHKG1)
CMY: 102934958(PHKG2) 102939493(PHKG1)
CPIC: 101932837(PHKG1) 101949847(PHKG2)
ACS: 100557980(phkg2)
PVT: 110084500(PHKG1) 110090073(PHKG2)
PBI: 103061914(PHKG2) 103065315(PHKG1)
GJA: 107111216(PHKG2) 107112491(PHKG1)
XLA: 108708334(phkg1.L) 373780(phkg1.S) 496328(phkg2.L)
XTR: 448255(phkg1) 779740(phkg2)
NPR: 108799187(PHKG1) 108803931(PHKG2)
DRE: 393937(phkg2) 554046(phkg1b) 565379(phkg1a)
IPU: 108273676(phkg2) 108280550(phkg1)
TRU: 101077385(phkg2) 101080204(phkg1)
LCO: 104923220(phkg2) 104936522(phkg1)
MZE: 101469795(phkg1) 101485765(phkg2)
OLA: 101165598(phkg2) 101167060(phkg1)
XMA: 102229601(phkg2) 102233585(phkg1)
PRET: 103474557(phkg1) 103481060(phkg2)
NFU: 107380364(phkg1) 107388054 107388073(phkg2)
KMR: 108237211(phkg2) 108246020(phkg1)
CSEM: 103378132(phkg1) 103381724(phkg2)
LCF: 108886377(phkg1) 108886752(phkg2)
SDU: 111219834(phkg2) 111228039(phkg1)
HCQ: 109525437(phkg1) 109530189(phkg2)
BPEC: 110154096 110159624(phkg2)
MALB: 109960264(phkg1) 109963558(phkg2)
OTW: 112223679 112265471(phkg1)
ELS: 105021305 105030287(phkg1)
SFM: 108922452(phkg1)
LCM: 102345800(PHKG1) 102362563
CMK: 103188445(phkg1)
CIN: 100182979
SPU: 582497
APLC: 110980692
SKO: 102804634
DME: Dmel_CG1830(PhKgamma)
DSI: Dsimw501_GD17041(Dsim_GD17041)
MDE: 101900257
AAG: 5578562
AEC: 105144123
ACEP: 105624549
PBAR: 105434370
CFO: 105255564
LHU: 105667336
PGC: 109856378
PCF: 106790636
NVI: 100117602
MDL: 103571859
TCA: 655530
DPA: 109543742
NVL: 108565553
BMOR: 101743489
PRAP: 110998330
HAW: 110380614
PXY: 105380550
API: 100168501
CLEC: 106665838
ZNE: 110830693
FCD: 110853985
TUT: 107369709
CEL: CELE_Y50D7A.3(Y50D7A.3)
CBR: CBG15712
BMY: Bm1_44555
TSP: Tsp_00128
CRG: 105317472
MYI: 110462867
OBI: 106871486
SHX: MS3_01719
EGL: EGR_05948
EPA: 110233083
ADF: 107344746
HMG: 100207615
AQU: 100641898
PIC: PICST_32412(PAK3)
SMIN: v1.2.023880.t1(symbB.v1.2.023880.t1)
SPAR: SPRG_03052
 » 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 20:150-7 (1956)
DOI:10.1016/0006-3002(56)90273-6
Reference
2  [PMID:13538949]
  Authors
KREBS EG, KENT AB, FISCHER EH.
  Title
The muscle phosphorylase b kinase reaction.
  Journal
J Biol Chem 231:73-83 (1958)
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 20:69-76 (1956)
DOI:10.1016/0006-3002(56)90264-5
Reference
4  [PMID:4029141]
  Authors
Nikolaropoulos S, Sotiroudis TG.
  Title
Phosphorylase kinase from chicken gizzard. Partial purification and characterization.
  Journal
Eur J Biochem 151:467-73 (1985)
DOI:10.1111/j.1432-1033.1985.tb09125.x
Reference
5  [PMID:1931956]
  Authors
Farrar YJ, Carlson GM.
  Title
Kinetic characterization of the calmodulin-activated catalytic subunit of phosphorylase kinase.
  Journal
Biochemistry 30:10274-9 (1991)
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 270:22283-9 (1995)
DOI:10.1074/jbc.270.38.22283
  Sequence
[ocu:100009297]
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 16:6646-58 (1997)
DOI:10.1093/emboj/16.22.6646
  Sequence
[ocu:100009297]
Other DBs
ExplorEnz - The Enzyme Database: 2.7.11.19
IUBMB Enzyme Nomenclature: 2.7.11.19
ExPASy - ENZYME nomenclature database: 2.7.11.19
BRENDA, the Enzyme Database: 2.7.11.19
CAS: 9001-88-1

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