KEGG   ENZYME: 2.7.11.2Help
Entry
EC 2.7.11.2                 Enzyme                                 

Name
[pyruvate dehydrogenase (acetyl-transferring)] kinase;
PDH kinase;
PDHK;
PDK;
PDK1;
PDK2;
PDK3;
PDK4;
pyruvate dehydrogenase kinase;
pyruvate dehydrogenase kinase (phosphorylating);
pyruvate dehydrogenase kinase activator protein;
STK1
Class
Transferases;
Transferring phosphorus-containing groups;
Protein-serine/threonine kinases
BRITE hierarchy
Sysname
ATP:[pyruvate dehydrogenase (acetyl-transferring)] phosphotransferase
Reaction(IUBMB)
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate [RN:R03449]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
[pyruvate dehydrogenase (acetyl-transferring)] [CPD:C01256]
Product
ADP [CPD:C00008];
[pyruvate dehydrogenase (acetyl-transferring)] phosphate [CPD:C01293]
Comment
The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring).
History
EC 2.7.11.2 created 1978 as EC 2.7.1.99, transferred 2005 to EC 2.7.11.2
Orthology
K00898  
pyruvate dehydrogenase kinase 2/3/4
K12077  
pyruvate dehydrogenase kinase isoform 1
Genes
HSA: 
5163(PDK1) 5164(PDK2) 5165(PDK3) 5166(PDK4)
PTR: 
459743(PDK1) 468402(PDK2) 472448(PDK4) 740576(PDK3)
PPS: 
100968174(PDK1) 100970620(PDK4) 100992308(PDK2) 100995647(PDK3)
GGO: 
101129032(PDK2) 101143387(PDK3) 101149286(PDK4) 101150048(PDK1)
PON: 
100174113(PDK2) 100435148(PDK4) 100442853(PDK1) 100462571(PDK3)
MCC: 
697772(PDK1) 698726(PDK4) 699394(PDK3) 704169
MCF: 
MMU: 
18604(Pdk2) 228026(Pdk1) 236900(Pdk3) 27273(Pdk4)
RNO: 
116551(Pdk1) 296849(Pdk3) 81530(Pdk2) 89813(Pdk4)
CGE: 
100758762(Pdk2) 100763413(Pdk4) 100770270(Pdk3) 100774056(Pdk1)
HGL: 
101698433(Pdk4) 101699582(Pdk3) 101699994(Pdk2) 101705587(Pdk1)
TUP: 
102468786(PDK4) 102469133(PDK2) 102483149(PDK3) 102499515(PDK1)
CFA: 
476828(PDK1) 480868(PDK3) 482310(PDK4) 491075(PDK2)
AML: 
FCA: 
101092256(PDK4) 101092705(PDK1) 101095314(PDK3) 101100013(PDK2)
PTG: 
BTA: 
507367(PDK4) 510841(PDK3) 524075(PDK2) 528655(PDK1)
BOM: 
102264999(PDK4) 102265648(PDK1) 102266253(PDK2) 102275065(PDK3)
PHD: 
102327657(PDK4) 102329508(PDK2) 102337867(PDK3) 102339076(PDK1)
CHX: 
102180838(PDK3) 102185217(PDK2) 102186251(PDK1) 102190015(PDK4)
OAS: 
101108725(PDK3) 101108929(PDK2) 101113205(PDK1) 101117752(PDK4)
SSC: 
100153858(PDK3) 100286778(PDK4) 100286871(PDK1) 100516037(PDK2)
CFR: 
BACU: 
LVE: 
103072788(PDK2) 103073094(PDK4) 103073975(PDK3) 103078387(PDK1)
ECB: 
100052078(PDK4) 100060791(PDK3) 100064091(PDK1) 100147514(PDK2)
MYB: 
102251531(PDK4) 102255458(PDK3) 102259213(PDK2) 102262215(PDK1)
MYD: 
102767099(PDK1) 102774306(PDK3) 102775297(PDK2) 102775518(PDK4)
PALE: 
102880150(PDK4) 102883688(PDK1) 102885302(PDK2) 102888523(PDK3)
MDO: 
100010271(PDK3) 100017644(PDK4) 100022514(PDK2) 100617164(PDK1)
SHR: 
OAA: 
100084173(PDK1) 100088087(PDK4)
GGA: 
418595(PDK3) 420570(PDK4) 425972(PDK1)
MGP: 
APLA: 
101790921(PDK1) 101793451(PDK3) 101796141(PDK4)
TGU: 
100218846(PDK1) 100226102(PDK3) 100230570(PDK4)
FAB: 
101810404(PDK4) 101812266(PDK2) 101812709(PDK1) 101819650(PDK3)
PHI: 
102100647(PDK3) 102101703(PDK1) 102105276(PDK2) 102107706(PDK4)
FPG: 
101913912(PDK4) 101915736(PDK2) 101921375(PDK3) 101925003(PDK1)
FCH: 
102050815(PDK1) 102050926(PDK3) 102054883(PDK4) 102055203(PDK2)
CLV: 
102092387(PDK2) 102093738(PDK3) 102097281(PDK4) 102098636(PDK1)
ASN: 
102370160(PDK4) 102375213(PDK2) 102384931(PDK1) 102385909(PDK3)
AMJ: 
102560712(PDK4) 102565725(PDK1) 102571137(PDK2) 102576429(PDK3)
PSS: 
102454133(PDK2) 102458098(PDK4) 102458322(PDK3) 102462980(PDK1)
CMY: 
102930569(PDK4) 102931646(PDK3) 102934483(PDK2) 102942305(PDK1)
ACS: 
100555492(pdk1) 100560978(pdk4) 100562544(pdk3) 100565122(pdk2)
PBI: 
103048669(PDK2) 103052031(PDK4) 103052758(PDK1) 103063932(PDK3)
XLA: 
XTR: 
100135009(pdk3) 100497838(pdk1) 448511(pdk4)
DRE: 
393971(pdk2b) 555840(pdk1) 560068(pdk3a) 561007(pdk4)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
103176918(pdk4) 103183848(pdk2) 103184837(pdk3)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
410424(Pdk)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_ZK370.5(pdhk-2)
CBR: 
CBG06929(Cbr-pdhk-2)
BMY: 
LOA: 
SMM: 
NVE: 
HMG: 
TAD: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
POPTR_0010s00440g(POPTRDRAFT_804707)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os03t0370000-01(Os03g0370000) Os07t0637300-01(Os07g0637300)
OBR: 
BDI: 
SBI: 
SORBI_01g034390(SORBIDRAFT_01g034390) SORBI_02g040610(SORBIDRAFT_02g040610)
ZMA: 
100193944 541677(pdlk1) 542603(pdlk2)
SITA: 
ATR: 
s00045p00085430(AMTR_s00045p00085430)
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
AGO: 
ERC: 
KLA: 
ZRO: 
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_836014(AO090026000452)
ANG: 
ANI_1_544024(An02g04000)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
DSQ: 
SHS: 
PCO: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT123518(AGABI1DRAFT_123518)
ABV: 
AGABI2DRAFT179568(AGABI2DRAFT_179568)
CPUT: 
SLA: 
UMA: 
PFP: 
MGL: 
PGR: 
MLR: 
WSE: 
MBR: 
ACAN: 
PTI: 
TPS: 
PIF: 
NGD: 
EHX: 
GTT: 
TBR: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:4401694]
  Authors
Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ.
  Title
-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart.
  Journal
Arch. Biochem. Biophys. 148 (1972) 327-42.
Reference
2  [PMID:3004826]
  Authors
Reed LJ, Damuni Z, Merryfield ML.
  Title
Regulation of mammalian pyruvate and branched-chain alpha-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation.
  Journal
Curr. Top. Cell. Regul. 27 (1985) 41-9.
Reference
3  [PMID:15629119]
  Authors
Tovar-Mendez A, Hirani TA, Miernyk JA, Randall DD.
  Title
Analysis of the catalytic mechanism of pyruvate dehydrogenase kinase.
  Journal
Arch. Biochem. Biophys. 434 (2005) 159-68.
  Sequence
[ath:AT3G06483]
Reference
4  [PMID:15491151]
  Authors
Bao H, Kasten SA, Yan X, Hiromasa Y, Roche TE.
  Title
Pyruvate dehydrogenase kinase isoform 2 activity stimulated by speeding up the rate of dissociation of ADP.
  Journal
Biochemistry. 43 (2004) 13442-51.
Reference
5  [PMID:12631265]
  Authors
Roche TE, Hiromasa Y, Turkan A, Gong X, Peng T, Yan X, Kasten SA, Bao H, Dong J.
  Title
Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1.
  Journal
Eur. J. Biochem. 270 (2003) 1050-6.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9074-01-5

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