KEGG   ENZYME: 1.17.4.2
Entry
EC 1.17.4.2                 Enzyme                                 
Name
ribonucleoside-triphosphate reductase (thioredoxin);
ribonucleotide reductase (ambiguous);
2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin 2'-oxidoreductase
Class
Oxidoreductases;
Acting on CH or CH2 groups;
With a disulfide as acceptor
Sysname
2'-deoxyribonucleoside-5'-triphosphate:thioredoxin-disulfide 2'-oxidoreductase
Reaction(IUBMB)
2'-deoxyribonucleoside 5'-triphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-triphosphate + thioredoxin [RN:R04315]
Reaction(KEGG)
Substrate
2'-deoxyribonucleoside 5'-triphosphate [CPD:C00677];
thioredoxin disulfide [CPD:C00343];
H2O [CPD:C00001]
Product
ribonucleoside 5'-triphosphate [CPD:C03802];
thioredoxin [CPD:C00342]
Comment
The enzyme, characterized from the bacterium Lactobacillus leichmannii, is similar to class II ribonucleoside-diphosphate reductase (cf. EC 1.17.4.1). However, it is specific for the triphosphate versions of its substrates. The enzyme contains an adenosylcobalamin cofactor that is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue. This radical attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. The disulfide bridge is reduced by the action of thioredoxin. cf. EC 1.1.98.6, ribonucleoside-triphosphate reductase (formate).
History
EC 1.17.4.2 created 1972, modified 2017
Pathway
ec00230  Purine metabolism
ec00240  Pyrimidine metabolism
ec01100  Metabolic pathways
Orthology
K00524  ribonucleotide reductase, class II
K00527  ribonucleoside-triphosphate reductase (thioredoxin)
Genes
DDIDDB_G0292654(ndrJ)
DPPDICPUDRAFT_51421
DFADFA_10847(ndrJ)
ACANACA1_356770
PIFPITG_02087
PSOJPHYSODRAFT_359310
SPARSPRG_12420
NGRNAEGRDRAFT_32325
NHLNhal_1612
NWRE3U44_15040
NSANitsa_1370
NISNIS_0814
BSEDDN745_16470
PCAYFRD00_17445
STEAC0679_13280(nrdJ)
LACLBA0041
LADLA14_0040
LAFSD55_0041(nrdJ)
LDBLdb0096(rtpR)
LBULBUL_0079
LDELDBND_0069(rtpR)
LDLLBU_0061
LGALGAS_1503
LHElhv_0042
LHLLBHH_0061
LHRR0052_00325
LHVlhe_0057(rtpR)
LHHLBH_0034
LHDHUO_01190
LAMLA2_00225
LAILAC30SC_00160
LAYLAB52_00155
LKEWANG_1429
LAWLACWKB8_0090
LAELBAT_0056
LGLAO203_02845
LAMYB1745_00235
LPWLpgJCM5343_14720(nrdD)
LKLDKL58_00360(nrdJ)
LAPIDKL56_00295(nrdJ)
LHSDLD54_00440(nrdJ)
LUUH4B44_00310(nrdJ)
LPAIGYM71_00475(nrdJ)
LIQKBW87_09305(nrdJ)
LCALSEI_2287
LCZLCAZH_2258
LCSLCBD_2467
LCELC2W_2450
LCWBN194_24230(rtpR)
LCLLOCK919_2525
LPQAF91_11350
LPILBPG_02206
LPAPLBPC_2218
LCBLCABL_24690(rtpR)
LCXLCA12A_1807
LRHLGG_02296(rtpR)
LRGLRHM_2207
LRLLC705_02286(rtpR)
LRALRHK_2294(nrdJ)
LROLOCK900_2258
LRCLOCK908_2350
LCHIKG086_10090(nrdJ)
LZEKG087_10725(nrdJ)
LRUHMPREF0538_20868(nrdJ)
LMALLM596_10920(nrdJ)
LBHLbuc_2266
LBNLBUCD034_2364(rtpR)
LPARFAM21731_01130
LKFDNL43_04465(nrdJ)
LHILG8J22_02668(rtpR)
LBRLVIS_1898
LBKLVISKB_1882
LKOABN16_08675
LACALAC1533_2224
LCYLC20004_00140
LPDAYR62_02815
LGNABM34_11885
LHIJP39_08335
LALWBTM29_06700
LALILA20249_05270
LFMLF20184_03520
LZHD1B17_09245(nrdJ)
LFTFG051_03425(nrdJ)
CPABG6534_02080(nrdJ)
WCFC6P13_01660(nrdJ)
WEIEQG49_03440(nrdJ)
PSEIGCE65_00680
SYCsyc0066_d
SYFSynpcc7942_1609
SYDSyncc9605_1277
SYESyncc9902_1200
SYGsync_1265
SYRSynRCC307_0954
SYXSynWH7803_1496
CYACYA_2169(nrdJ)
CYBCYB_0734(nrdJ)
SYNESyn6312_1041
SYNPSyn7502_00172
SYNKKR100_09200
SYNRKR49_02590
SYNDKR52_10175
SYHSyncc8109_1411(nrdJ)
SYNWSynWH8103_01295(nrdJ)
SYNCCB0101_01490(nrdJ)
SYNYBM449_03495
DSLDacsa_2534
SYWSYNW1147(nrdJ)
CGCCyagr_0672
CYICBM981_1075(nrdJ)
PMAPro_0815
PMMPMM0661(nrdJ)
PMTPMT_0793
PMNPMN2A_0093
PMIPMT9312_0661
PMBA9601_07161(nrdJ)
PMCP9515_07341(nrdJ)
PMFP9303_14171(nrdJ)
PMGP9301_07141(nrdJ)
PMHP9215_07461(nrdJ)
PMJP9211_07711(nrdJ)
PMENATL1_07181(nrdJ)
PRCEW14_0735
PRMEW15_0762
CMPCha6605_5310
TVNNIES2134_112260
SLWBRW62_01085
TELtll1327
THNNK55_03120(nrdJ)
THECFFX45_11355(nrdJ)
LENLEP3755_23730
LETO77CONTIG1_02868(rtpR)
LBOLBWT_19490
KOVK9N68_17595(nrdJ)
LSCKIK02_18800(nrdJ)
LSKJ5X98_14660(nrdJ)
HHGXM38_000430(rtpR)
PSEUPse7367_0353
PSERABRG53_0545
THEUHPC62_16675(nrdJ)
GLPGlo7428_4669
HAOPCC7418_0282
TERTery_0425
OXYHCG48_04430
MVAGD0A34_15735(nrdJ)
GEIGEI7407_0881
OACOscil6304_0998
ANAall4035
NOSNos7107_2758
NOPNos7524_1315
NONNOS3756_14430
NFLCOO91_06145
NOECLI64_18990
NSHGXM_06230
AVAAva_1670
NAZAazo_1083
ANNEH233_08600(nrdJ)
RSINB6N60_04990
CALOCal7507_4553
CALTCal6303_1739
CALHIJ00_25960
CALNNIES2098_59300(nrdJ)
RIVRiv7116_1234
FISFIS3754_10960
NSPHBDGGKGIB_00893(rtpR)
DOUBMF77_03053(rtpR_2)
DFSHGD76_08910(nrdJ)
DHTNG743_22100
AFLOHEQ12_05295(nrdJ)
CTHEChro_0760
BPITBPIT_35840
JETL3J17_06935
FLMMY04_3968
FLLEI427_01965
FYAKMW28_16600
FKAKM029_08790
AUEC5O00_07325
LOKILokiarch_02190(rtpR_1) Lokiarch_49710(rtpR_2)
PSYTDSAG12_00884
 » show all
Reference
1  [PMID:14299643]
  Authors
BLAKLEY RL.
  Title
COBAMIDES AND RIBONUCLEOTIDE REDUCTION. I. COBAMIDE STIMULATION OF RIBONUCLEOTIDE REDUCTION IN EXTRACTS OF LACTOBACILLUS LEICHMANNII.
  Journal
J Biol Chem 240:2173-80 (1965)
Reference
2  [PMID:5924645]
  Authors
Goulian M, Beck WS.
  Title
Purification and properties of cobamide-dependent ribonucleotide reductase from Lactobacillus leichmannii.
  Journal
J Biol Chem 241:4233-42 (1966)
Reference
3  [PMID:7014560]
  Authors
Stubbe J, Ackles D, Segal R, Blakley RL
  Title
On the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii. Evidence for 3' C--H bond cleavage.
  Journal
J Biol Chem 256:4843-6 (1981)
Reference
4  [PMID:3512563]
  Authors
Ashley GW, Harris G, Stubbe J
  Title
The mechanism of Lactobacillus leichmannii ribonucleotide reductase. Evidence for 3' carbon-hydrogen bond cleavage and a unique role for coenzyme B12.
  Journal
J Biol Chem 261:3958-64 (1986)
Reference
5  [PMID:9818192]
  Authors
Lawrence CC, Stubbe J
  Title
The function of adenosylcobalamin in the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii.
  Journal
Curr Opin Chem Biol 2:650-5 (1998)
DOI:10.1016/S1367-5931(98)80097-5
Reference
6  [PMID:9930982]
  Authors
Licht SS, Booker S, Stubbe J
  Title
Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation.
  Journal
Biochemistry 38:1221-33 (1999)
DOI:10.1021/bi981885i
Other DBs
ExplorEnz - The Enzyme Database: 1.17.4.2
IUBMB Enzyme Nomenclature: 1.17.4.2
ExPASy - ENZYME nomenclature database: 1.17.4.2
BRENDA, the Enzyme Database: 1.17.4.2
CAS: 9068-66-0

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