KEGG   ENZYME: 2.5.1.58Help
Entry
EC 2.5.1.58                 Enzyme                                 

Name
protein farnesyltransferase;
FTase
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy
Sysname
farnesyl-diphosphate:protein-cysteine farnesyltransferase
Reaction(IUBMB)
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate [RN:R09844]
Reaction(KEGG)
Substrate
farnesyl diphosphate [CPD:C00448];
protein-cysteine [CPD:C20119]
Product
S-farnesyl protein [CPD:C20120];
diphosphate [CPD:C00013]
Comment
This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity.
History
EC 2.5.1.58 created 2003
Pathway
ec00900  Terpenoid backbone biosynthesis
ec01130  Biosynthesis of antibiotics
Orthology
K05954  protein farnesyltransferase subunit beta
K05955  protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Genes
HSA: 2339(FNTA) 2342(FNTB)
PTR: 452971(FNTB) 472929(FNTA)
PPS: 100991890(FNTB) 103786897(FNTA)
GGO: 101147861(FNTA) 101150420(FNTB)
PON: 100436184(FNTB) 100448439(FNTA)
NLE: 100603548(FNTB) 100605797(FNTA)
MCC: 708129(FNTB) 712681(FNTA)
MCF: 101865967(FNTB) 101866500(FNTA)
CSAB: 103215701(FNTA) 103229180(FNTB)
RRO: 104668310(FNTA) 104678437(FNTB)
RBB: 108542421(FNTB)
CJC: 100392598(FNTB) 100401677(FNTA)
SBQ: 101053282(FNTB) 104649982(FNTA)
MMU: 110606(Fntb) 14272(Fnta)
RNO: 25318(Fnta) 64511(Fntb)
CGE: 100752221(Fntb) 100752295(Fnta)
NGI: 103749278(Fntb)
HGL: 101703640(Fnta) 101703774(Fntb)
CCAN: 109691132(Fntb) 109699820(Fnta)
OCU: 100341143 100343931(FNTB) 100347188(FNTA)
TUP: 102479775(FNTB) 102494685(FNTA)
CFA: 475566(FNTA) 490735(FNTB)
AML: 100467230(FNTA) 100474526
UMR: 103674342 103677044(FNTA)
ORO: 101376890(FNTA) 101383702(FNTB) 101383786
FCA: 101088759(FNTB) 101097062(FNTA)
PTG: 102957564(FNTA) 102966415(FNTB)
AJU: 106971334(FNTB) 106990022(FNTA)
BTA: 281169(FNTA) 327686(FNTB)
BOM: 102272299(FNTA) 102287965(FNTB)
BIU: 109553498(FNTA) 109565251(FNTB)
PHD: 102330315(FNTB) 102332237(FNTA)
CHX: 102189488(FNTB) 102191016(FNTA)
OAS: 100302086(FNTA) 101110335(FNTB)
SSC: 100512293(FNTB) 100627556(FNTA)
CFR: 102511020(FNTA) 102522965(FNTB)
CDK: 105086183 105094300(FNTA)
BACU: 102999003(FNTB) 103014092(FNTA)
LVE: 103074104(FNTB) 103085981(FNTA)
OOR: 101277224(FNTB) 101288631(FNTA)
ECB: 100052486(FNTB) 100053704(FNTA)
EPZ: 103541355(FNTA) 103550215(FNTB)
EAI: 106828969(FNTA) 106844888(FNTB)
MYB: 102255519(FNTA) 102261986(FNTB)
MYD: 102751880(FNTB) 102770189(FNTA)
HAI: 109382065 109386282(FNTA)
RSS: 109442237 109448276(FNTB) 109452851(FNTA)
PALE: 102881721(FNTB) 102890666(FNTA)
LAV: 100655632(FNTB) 100669104(FNTA)
MDO: 100027938(FNTB) 100617990(FNTA)
SHR: 100916157(FNTB) 100924354(FNTA)
OAA: 100078580(FNTA)
GGA: 100857683(FNTB) 427299(FNTA)
MGP: 100544213(FNTA) 100548337
APLA: 101793836(FNTA)
ACYG: 106040419(FNTA)
TGU: 100222812(FNTA) 100223864
GFR: 102031891(FNTA) 102043195(FNTB)
FAB: 101810421(FNTB) 101814503(FNTA)
PHI: 102102894(FNTB) 102111175(FNTA)
PMAJ: 107198168(FNTA) 107205595
CCAE: 111940897(FNTA) 111945042
CCW: 104689741(FNTA) 104693013
FPG: 101913248(FNTA) 101920206(FNTB)
FCH: 102046284(FNTA) 102052180 102059349(FNTB)
EGZ: 104126429(FNTA)
ASN: 102382443(FNTA) 102385137
AMJ: 102564152(FNTA) 102574457(FNTB)
PSS: 102452430(FNTA) 102459340
CMY: 102937672(FNTB) 102940529
CPIC: 101934158(FNTA) 101938834(FNTB)
ACS: 100559827 100561851(fnta)
PVT: 110083168(FNTA) 110085642
PBI: 103049019 103051193(FNTA)
GJA: 107120943(FNTA) 107121947
XLA: 100137632(fnta.S) 108699724(fntb.S) 447605(fntb.L)
XTR: 100144648(fnta) 550012(fntb)
NPR: 108796770 108804918(FNTA)
DRE: 323500(fntb) 555882(fnta)
IPU: 108257588 108268629(fnta)
AMEX: 103026998(fnta) 103033540
TRU: 101076206(fnta) 101079983
NCC: 104942305(fnta) 104949856
MZE: 101468735(fnta) 101479885
OLA: 101160126 101160920(fnta)
XMA: 102234643(fnta) 102235994
PRET: 103457641 103471041(fnta)
NFU: 107377823 107381432(fnta)
KMR: 108228747(fnta) 108233508
CSEM: 103381205 103391301(fnta)
LCF: 108878782(fnta) 108887265
SDU: 111216443 111226657(fnta)
HCQ: 109515791(fnta) 109523733
BPEC: 110159349 110166430(fnta)
MALB: 109957583(fnta) 109962295
ELS: 105006791(fnta) 105024336
SFM: 108919508 108938728(fnta)
LCM: 102349666(FNTA) 102350945(FNTB)
CMK: 103175221 103191504(fnta)
CIN: 445680(fta)
DME: Dmel_CG17565(CG17565) Dmel_CG2976(Fnta)
DSI: Dsimw501_GD19096(Dsim_GD19096) Dsimw501_GD22689(Dsim_GD22689)
NVI: 100123894
BMOR: 692501(Fnta) 692537(Fntb)
API: 100166879 100167417(Fnta)
CEL: CELE_F23B12.6(fntb-1) CELE_R02D3.5(fnta-1)
CBR: CBG01666 CBG04611(Cbr-tag-114)
ADF: 107335525
ATH: AT3G59380(FTA) AT5G40280(ERA1)
GMX: 100306703(GMERA1B) 100790130 100811502 100814543(GMERA1A)
LJA: Lj0g3v0089459.1(Lj0g3v0089459.1) Lj2g3v1014160.1(Lj2g3v1014160.1)
SLY: 544036(FTA) 544037(FTB)
NTA: 107777651 107798306 107814428(Ntalpha) 107827532(NtbetaF)
DOSA: Os09t0514400-01(Os09g0514400)
ATS: 109744376(LOC109744376) 109773598(LOC109773598) 109778677(LOC109778677)
ZMA: 100272584(pco074498b) 100273635
SCE: YDL090C(RAM1) YKL019W(RAM2)
KMX: KLMA_20389(RAM1) KLMA_60145(RAM2)
NCS: NCAS_0B05820(NCAS0B05820) NCAS_0H03470(NCAS0H03470)
NDI: NDAI_0B03130(NDAI0B03130) NDAI_0C00210(NDAI0C00210)
TPF: TPHA_0C03780(TPHA0C03780) TPHA_0N01840(TPHA0N01840)
TBL: TBLA_0A00700(TBLA0A00700) TBLA_0B09490(TBLA0B09490)
TDL: TDEL_0B07560(TDEL0B07560) TDEL_0G02960(TDEL0G02960)
KAF: KAFR_0A06950(KAFR0A06950) KAFR_0C03850(KAFR0C03850)
PIC: PICST_55783(RAM2) PICST_82404(RAM1)
SLB: AWJ20_185(RAM2) AWJ20_887(RAM1)
NTE: NEUTE1DRAFT144524(NEUTE1DRAFT_144524) NEUTE1DRAFT88206(NEUTE1DRAFT_88206)
ANG: ANI_1_1988184(An04g06620) ANI_1_462184(An04g02210)
CIM: CIMG_05727 CIMG_12864(CIMG00563)
PBL: PAAG_07086 PAAG_11163(PAAG_00717) PAAG_11164
SPO: SPAC17G6.04c(cpp1) SPAPB1A10.04c(cwp1)
ABP: AGABI1DRAFT115274(AGABI1DRAFT_115274) AGABI1DRAFT61805(AGABI1DRAFT_61805)
ABV: AGABI2DRAFT194236(AGABI2DRAFT_194236) AGABI2DRAFT210804(AGABI2DRAFT_210804)
DDI: DDB_G0270948(fntB) DDB_G0283053(fntA)
DFA: DFA_05584(fntA) DFA_10414(fntB)
EHI: EHI_006190(83.t00031) EHI_074760(288.t00007)
PYO: PY17X_0903000(PY02409)
TPV: TP02_0810
BBO: BBOV_III002550(17.m07246) BBOV_III004550(17.m07408)
CPV: cgd6_2510
SMIN: v1.2.028464.t1(symbB.v1.2.028464.t1)
 » show all
Taxonomy
Reference
1  [PMID:7756316]
  Authors
Furfine ES, Leban JJ, Landavazo A, Moomaw JF, Casey PJ.
  Title
Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release.
  Journal
Biochemistry 34:6857-62 (1995)
Reference
2  [PMID:8621375]
  Authors
Casey PJ, Seabra MC.
  Title
Protein prenyltransferases.
  Journal
J Biol Chem 271:5289-92 (1996)
DOI:10.1074/jbc.271.10.5289
Reference
3  [PMID:9657673]
  Authors
Long SB, Casey PJ, Beese LS.
  Title
Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate.
  Journal
Biochemistry 37:9612-8 (1998)
DOI:10.1021/bi980708e
  Sequence
[rno:25318 64511]
Reference
4  [PMID:11591144]
  Authors
Micali E, Chehade KA, Isaacs RJ, Andres DA, Spielmann HP.
  Title
Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups.
  Journal
Biochemistry 40:12254-65 (2001)
DOI:10.1021/bi011133f
Reference
5  [PMID:12374986]
  Authors
Long SB, Casey PJ, Beese LS.
  Title
Reaction path of protein farnesyltransferase at atomic resolution.
  Journal
Nature 419:645-50 (2002)
DOI:10.1038/nature00986
Reference
6
  Authors
Gibbs, R.A.
  Title
Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis.
  Journal
In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, p. 31-118.
Other DBs
ExplorEnz - The Enzyme Database: 2.5.1.58
IUBMB Enzyme Nomenclature: 2.5.1.58
ExPASy - ENZYME nomenclature database: 2.5.1.58
BRENDA, the Enzyme Database: 2.5.1.58
CAS: 131384-38-8

KEGG   ENZYME: 2.5.1.59Help
Entry
EC 2.5.1.59                 Enzyme                                 

Name
protein geranylgeranyltransferase type I;
GGTase-I;
GGTaseI
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy
Sysname
geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Reaction(IUBMB)
geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Substrate
geranylgeranyl diphosphate [CPD:C00353];
protein-cysteine [CPD:C20119]
Product
S-geranylgeranyl-protein;
diphosphate [CPD:C00013]
Comment
This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.
History
EC 2.5.1.59 created 2003
Orthology
K05955  protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
K11713  geranylgeranyl transferase type-1 subunit beta
Genes
HSA: 2339(FNTA) 5229(PGGT1B)
PTR: 471600(PGGT1B) 472929(FNTA)
PPS: 100989189(PGGT1B) 103786897(FNTA)
GGO: 101146731(PGGT1B) 101147861(FNTA)
PON: 100436505(PGGT1B) 100448439(FNTA)
NLE: 100592053(PGGT1B) 100605797(FNTA)
MCC: 696437(PGGT1B) 712681(FNTA)
MCF: 101866500(FNTA) 102138022(PGGT1B)
CSAB: 103215701(FNTA) 103244358(PGGT1B)
RRO: 104657192(PGGT1B) 104668310(FNTA)
RBB: 108524203(PGGT1B)
CJC: 100401677(FNTA) 100411484(PGGT1B)
SBQ: 101045513(PGGT1B) 104649982(FNTA)
MMU: 14272(Fnta) 225467(Pggt1b)
RNO: 25318(Fnta) 81746(Pggt1b)
CGE: 100752295(Fnta) 100759155(Pggt1b)
NGI: 103727411(Pggt1b)
HGL: 101703640(Fnta) 101723510(Pggt1b)
CCAN: 109697315(Pggt1b) 109699820(Fnta)
OCU: 100344716(PGGT1B) 100347188(FNTA)
TUP: 102483233(PGGT1B) 102494685(FNTA)
CFA: 475566(FNTA) 481440(PGGT1B)
AML: 100467230(FNTA) 100476901(PGGT1B)
UMR: 103677044(FNTA) 103679960(PGGT1B)
ORO: 101376890(FNTA) 101382332(PGGT1B) 101383786
FCA: 101089829(PGGT1B) 101097062(FNTA)
PTG: 102951684(PGGT1B) 102957564(FNTA)
AJU: 106978928(PGGT1B) 106990022(FNTA)
BTA: 281169(FNTA) 509322(PGGT1B)
BOM: 102271879(PGGT1B) 102272299(FNTA)
BIU: 109553498(FNTA) 109564164(PGGT1B)
PHD: 102324598(PGGT1B) 102332237(FNTA)
CHX: 102183603(PGGT1B) 102191016(FNTA)
OAS: 100302086(FNTA) 101123045(PGGT1B)
SSC: 100520066(PGGT1B) 100627556(FNTA)
CFR: 102511020(FNTA) 102511063(PGGT1B)
CDK: 105094300(FNTA) 105095372(PGGT1B)
BACU: 103004097(PGGT1B) 103014092(FNTA)
LVE: 103085770(PGGT1B) 103085981(FNTA)
OOR: 101278467(PGGT1B) 101288631(FNTA)
ECB: 100053704(FNTA) 100064254(PGGT1B)
EPZ: 103541355(FNTA) 103546974(PGGT1B)
EAI: 106828969(FNTA) 106832147(PGGT1B)
MYB: 102242187(PGGT1B) 102255519(FNTA)
MYD: 102770189(FNTA) 102773769(PGGT1B)
HAI: 109378866 109386282(FNTA) 109387388(PGGT1B)
RSS: 109442237 109445428(PGGT1B) 109452851(FNTA)
PALE: 102883059(PGGT1B) 102890666(FNTA)
LAV: 100662535(PGGT1B) 100669104(FNTA)
MDO: 100016343(PGGT1B) 100617990(FNTA)
SHR: 100924354(FNTA) 100928606(PGGT1B)
OAA: 100076094(PGGT1B) 100078580(FNTA)
GGA: 427299(FNTA) 770633(PGGT1B)
MGP: 100544213(FNTA) 100547395(PGGT1B)
CJO: 107306423 107306699(PGGT1B)
APLA: 101792505(PGGT1B) 101793836(FNTA)
ACYG: 106040419(FNTA) 106046545(PGGT1B)
TGU: 100222663(PGGT1B) 100222812(FNTA)
GFR: 102031891(FNTA) 102040390(PGGT1B)
FAB: 101807115(PGGT1B) 101814503(FNTA)
PHI: 102111175(FNTA) 102111835(PGGT1B)
PMAJ: 107198168(FNTA) 107216448(PGGT1B)
CCAE: 111940897(FNTA) 111941283(PGGT1B)
CCW: 104689741(FNTA) 104690464(PGGT1B)
FPG: 101913248(FNTA) 101914299(PGGT1B)
FCH: 102046284(FNTA) 102051911(PGGT1B) 102052180
CLV: 102094236(PGGT1B) 102098098
EGZ: 104124251(PGGT1B) 104126429(FNTA)
AAM: 106482499
ASN: 102378457(PGGT1B) 102382443(FNTA)
AMJ: 102564152(FNTA) 102575535(PGGT1B)
PSS: 102445929(PGGT1B) 102452430(FNTA)
CMY: 102940529 102941621(PGGT1B)
CPIC: 101934158(FNTA) 101937363(PGGT1B)
ACS: 100556324(pggt1b) 100561851(fnta)
PVT: 110072043(PGGT1B) 110083168(FNTA)
PBI: 103051193(FNTA) 103055655(PGGT1B)
GJA: 107114710(PGGT1B) 107120943(FNTA)
XLA: 100137632(fnta.S) 734580(pggt1b.S)
XTR: 100144648(fnta) 493499(pggt1b)
NPR: 108789760(PGGT1B) 108804918(FNTA)
DRE: 555882(fnta) 570808(pggt1b)
IPU: 108265836(pggt1b) 108268629(fnta)
AMEX: 103026998(fnta) 103043070(pggt1b)
TRU: 101061300(pggt1b) 101076206(fnta)
LCO: 104919278(pggt1b) 104920555(fnta) 109141898
NCC: 104942305(fnta) 104949733(pggt1b)
MZE: 101468735(fnta) 101483452(pggt1b)
OLA: 101160920(fnta) 101167874(pggt1b)
XMA: 102233377(pggt1b) 102234643(fnta)
PRET: 103470195(pggt1b) 103471041(fnta)
NFU: 107381432(fnta) 107394052(pggt1b)
KMR: 108228747(fnta) 108234480(pggt1b)
LCF: 108878646(pggt1b) 108878782(fnta)
SDU: 111226657(fnta) 111230878(pggt1b)
HCQ: 109515791(fnta) 109526318(pggt1b)
BPEC: 110156386(pggt1b) 110166430(fnta)
MALB: 109957583(fnta) 109961513(pggt1b)
ELS: 105006791(fnta) 105014617(pggt1b)
SFM: 108937973(pggt1b) 108938728(fnta)
LCM: 102349666(FNTA) 102359482(PGGT1B)
CMK: 103181137(pggt1b) 103191504(fnta)
CIN: 100186051 445680(fta)
DME: Dmel_CG2976(Fnta) Dmel_CG3469(betaggt-I)
DSI: Dsimw501_GD22689(Dsim_GD22689) Dsimw501_GD23309(Dsim_GD23309)
BMOR: 100463493 692501(Fnta)
API: 100164617 100167417(Fnta)
TUT: 107371809
CEL: CELE_R02D3.5(fnta-1) CELE_Y48E1B.3(Y48E1B.3)
ADF: 107344583
ATH: AT2G39550(PGGT-I) AT3G59380(FTA)
LJA: Lj0g3v0089459.1(Lj0g3v0089459.1) Lj1g3v3219190.1(Lj1g3v3219190.1)
SLY: 101263319 544036(FTA)
DOSA: Os01t0150100-01(Os01g0150100) Os09t0514400-01(Os09g0514400)
ATS: 109738989(LOC109738989) 109744376(LOC109744376) 109773598(LOC109773598)
ZMA: 100273635
MNG: MNEG_5127
APRO: F751_3684
SCE: YGL155W(CDC43) YKL019W(RAM2)
KMX: KLMA_60145(RAM2) KLMA_80107(CDC43)
NCS: NCAS_0D00730(NCAS0D00730) NCAS_0H03470(NCAS0H03470)
NDI: NDAI_0C00210(NDAI0C00210) NDAI_0H03430(NDAI0H03430)
TPF: TPHA_0G00890(TPHA0G00890) TPHA_0N01840(TPHA0N01840)
TBL: TBLA_0A00700(TBLA0A00700) TBLA_0B06120(TBLA0B06120)
TDL: TDEL_0B07560(TDEL0B07560) TDEL_0G02420(TDEL0G02420)
KAF: KAFR_0B04650(KAFR0B04650) KAFR_0C03850(KAFR0C03850)
PIC: PICST_55783(RAM2) PICST_79863(CDC43)
CDU: CD36_08990 CD36_30310(CDC43)
SLB: AWJ20_185(RAM2) AWJ20_253(CDC43)
NTE: NEUTE1DRAFT144524(NEUTE1DRAFT_144524) NEUTE1DRAFT67673(NEUTE1DRAFT_67673)
ANG: ANI_1_1458164(An18g06340) ANI_1_462184(An04g02210)
PBL: PAAG_00914 PAAG_11163(PAAG_00717) PAAG_11164
SPO: SPAC2E1P5.04c(cwg2) SPAPB1A10.04c(cwp1)
ABP: AGABI1DRAFT100190(AGABI1DRAFT_100190) AGABI1DRAFT115274(AGABI1DRAFT_115274)
ABV: AGABI2DRAFT194236(AGABI2DRAFT_194236) AGABI2DRAFT72409(AGABI2DRAFT_72409)
MGL: MGL_0707
DFA: DFA_02723 DFA_05584(fntA)
EHI: EHI_074760(288.t00007) EHI_077230(40.t00014)
TAN: TA17870
BBO: BBOV_III002550(17.m07246)
CPV: cgd6_2510
SMIN: v1.2.028464.t1(symbB.v1.2.028464.t1)
 » show all
Taxonomy
Reference
1  [PMID:8621375]
  Authors
Casey PJ, Seabra MC.
  Title
Protein prenyltransferases.
  Journal
J Biol Chem 271:5289-92 (1996)
DOI:10.1074/jbc.271.10.5289
Reference
2  [PMID:9003382]
  Authors
Zhang FL, Casey PJ.
  Title
Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I.
  Journal
Biochem J 320 ( Pt 3):925-32 (1996)
Reference
3
  Authors
Gibbs, R.A.
  Title
Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis.
  Journal
In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, p. 31-118.
Other DBs
ExplorEnz - The Enzyme Database: 2.5.1.59
IUBMB Enzyme Nomenclature: 2.5.1.59
ExPASy - ENZYME nomenclature database: 2.5.1.59
BRENDA, the Enzyme Database: 2.5.1.59
CAS: 135371-29-8

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