Entry
Name
ribonuclease T1;
barnase;
bacterial ribonuclease Sa;
guanyloribonuclease;
Aspergillus oryzae ribonuclease;
RNase N1;
RNase N2;
ribonuclease N3;
ribonuclease U1;
ribonuclease F1;
ribonuclease Ch;
ribonuclease PP1;
ribonuclease SA;
RNase F1;
ribonuclease C2;
binase;
RNase Sa;
guanyl-specific RNase;
RNase G;
RNase T1;
ribonuclease guaninenucleotido-2'-transferase (cyclizing);
ribonuclease N1
Class
Lyases;
Phosphorus-oxygen lyases;
Phosphorus-oxygen lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
[RNA]-guanosine 5'-hydroxy-ribonucleotide-3'-[RNA fragment]-lyase (cyclicizing; [RNA fragment]-3'-guanosine-2',3'-cyclophosphate-forming and hydrolysing)
Reaction(IUBMB)
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment] (overall reaction);
(1a) [RNA] containing guanosine = [RNA fragment]-3'-guanosine-2',3'-cyclophosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment];
(1b) [RNA fragment]-3'-guanosine-2',3'-cyclophosphate + H2O = [RNA fragment]-3'-guanosine-3'-phosphate
Substrate
[RNA] containing guanosine;
H2O [CPD:
C00001 ];
[RNA fragment]-3'-guanosine-2',3'-cyclophosphate
Product
[RNA fragment]-3'-guanosine-3'-phosphate;
5'-hydroxy-ribonucleotide-3'-[RNA fragment];
[RNA fragment]-3'-guanosine-2',3'-cyclophosphate
Comment
A family of related enzymes found in some fungi and bacteria. The enzyme is specific for cleavage at the 3'-phosphate group of guanosine in single stranded RNA, and catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending in Gp with 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses these cyclic compounds in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
History
EC 4.6.1.24 created 1961 as EC 3.1.4.8, transferred 1965 to EC 2.7.7.26, reinstated 1972 as EC 3.1.4.8, transferred 1978 to EC 3.1.27.3, transferred 2020 to EC 4.6.1.24
Orthology
Genes
XPH : XppCFBP6546_01080(XppCFBP6546P_01080)
XTS : AB3X08_09515 AB3X08_20555
LGU : LG3211_1584 LG3211_5211(rnaSA3)
LEZ : GLE_0078 GLE_1561(rnaSA)
LSF : I8J32_004270 I8J32_014400
REH : H16_A3152(h16_A3152)
REU : Reut_A2846 Reut_A2926
BYI : BYI23_A022160 BYI23_C013600
BUM : AXG89_08445 AXG89_34895
BUI : AX768_01615 AX768_17605
BURT : BTHE68_21050 BTHE68_46070
BXB : DR64_2733(rnaSA) DR64_6839
BGE : BC1002_2657 BC1002_6629
BPY : Bphyt_3396 Bphyt_4699
BCAI : K788_0005378 K788_0006890
PSPW : BJG93_15350 BJG93_30445
PARB : CJU94_07975 CJU94_26795
PHS : C2L64_15540 C2L64_29660
PTER : C2L65_13445 C2L65_18690
PGP : CUJ91_15350 CUJ91_33625
PCJ : CUJ87_14715 CUJ87_25890
PGIS : I6I06_14445 I6I06_18320
PACP : FAZ97_01865 FAZ97_34265
PEW : KZJ38_04225 KZJ38_18330
PDIO : PDMSB3_1575.1 PDMSB3_3815(rnaSA)
PBRY : NDK50_18115 NDK50_29080
PSAA : QEN71_09445 QEN71_27025
PKF : RW095_17315 RW095_32615
PLAD : PPGU16_27470 PPGU16_56240
PAZZ : PBP221_27850 PBP221_40980
CABA : SBC2_05100 SBC2_45720
BUO : BRPE64_ACDS23380 BRPE64_CCDS05280
CABK : NK8_23410 NK8_49150
BUE : BRPE67_ACDS22920 BRPE67_CCDS12890
PVAC : HC248_03513(rnaSA3)
THAG : CKCBHOJB_02970(rnaSA3)
AAGG : ETAA8_24360(rnaSA) ETAA8_54910
PCM : AY601_1714 AY601_3741
MSAL : DSM43276_02191(rnaSA)
CDIP : ERS451417_01716(rnaSA)
CMIN : NCTC10288_00650(rnaSA)
CRL : NCTC7448_00112(rnaSA)
CFAC : CFAEC_09895(rnaSA3)
NBR : O3I_005290 O3I_030835
NOZ : DMB37_09555 DMB37_26280
NAH : F5544_06225 F5544_36930
NWL : NWFMUON74_62320 NWFMUON74_62720
NVU : V7968_12680 V7968_38665
TSM : ASU32_01995 ASU32_18315
SMA : SAVERM_1991 SAVERM_6882
SHO : SHJGH_2658 SHJGH_7062
SCI : B446_07590 B446_29315
STRE : GZL_02588 GZL_07232
SLC : SL103_12225 SL103_25070
SAMB : SAM23877_5974(rnaSA)
SCX : AS200_11225 AS200_36345
SRW : TUE45_01873(rnaSA3_1) TUE45_06871(rnaSA3_2)
STRF : ASR50_06930 ASR50_28655
SLE : sle_14300(sle_14300)
STRT : A8713_04970 A8713_26085
SGS : AVL59_13165 AVL59_33805
SKY : D0C37_04340 D0C37_28975
SALW : CP975_05435 CP975_29375
SCAD : DN051_09955 DN051_31365
SNR : SNOUR_11040 SNOUR_33125
SALU : DC74_1917 DC74_6422
SALL : SAZ_10165 SAZ_32260
SPUN : BFF78_09945 BFF78_34255
SGV : B1H19_09305 B1H19_32025
SALF : SMD44_01499 SMD44_06882
SALJ : SMD11_1417 SMD11_4596 SMD11_5205
SLX : SLAV_03455(rnaSA3) SLAV_30190
STRO : STRMOE7_07870 STRMOE7_30545
SGD : ELQ87_02470 ELQ87_07185 ELQ87_32470
SAST : CD934_05215 CD934_28420
SNQ : CP978_06870 CP978_27885
SKA : CP970_07885 CP970_36560
SVN : CP980_02280 CP980_27450
SRK : FGW37_07560 FGW37_25960
SGAL : CP966_05680 CP966_29400
SVR : CP971_04130 CP971_23065
SPAD : DVK44_05220 DVK44_06015
SFY : GFH48_10180 GFH48_33205
SAQU : EJC51_09895 EJC51_37510
SGF : HEP81_01722 HEP81_06318
SSEO : D0Z67_04230 D0Z67_23655
SRIM : CP984_07660 CP984_34355
SSUB : CP968_06270 CP968_27265
SSPB : CP982_08640 CP982_32725
SPLA : CP981_06985 CP981_30835
SBRO : GQF42_09925 GQF42_33625
SHUN : DWB77_00225 DWB77_05719(rnaSA3) DWB77_06291
SDW : K7C20_06095 K7C20_29465
SAUH : SU9_005035 SU9_028325
SMOB : J7W19_06845 J7W19_25795
SROI : IAG44_07940 IAG44_33270
SXN : IAG42_06810 IAG42_29780
SHK : J2N69_05370 J2N69_30790
SANU : K7396_07720 K7396_29735
SDD : D9753_06740 D9753_29585
SINE : KI385_09400 KI385_35425
SLF : JEQ17_10925 JEQ17_38445
SAOV : G3H79_06395 G3H79_31440
SDUR : M4V62_09860 M4V62_34765
SRUG : F0345_03330 F0345_24680
STAA : LDH80_29215 LDH80_32225
SNIG : HEK616_20940 HEK616_48620
SVIO : HWN34_03720 HWN34_27195
SCIR : STRCI_001513 STRCI_006510
SLON : LGI35_10485 LGI35_34055
STUD : STRTU_001340 STRTU_005972
STEE : F3L20_10530 F3L20_13385
SENG : OJ254_21155 OJ254_29045
SYUN : MOV08_10840 MOV08_33485
SCYN : N8I84_08010 N8I84_31640
SOV : QZH56_06010 QZH56_28130
SHAU : K9S39_11475 K9S39_35860
SFP : QUY26_07440 QUY26_33825
SINN : ABB07_07235 ABB07_31470
STPB : QR97_29850 QR97_32270
SRPA : HEP86_08165 HEP86_32070
SMIB : SMIR_05405 SMIR_32630
SCAJ : O1G22_08825 O1G22_34455
STRW : QHG49_07455 QHG49_28875
STRL : HEP84_12280 HEP84_40135
STSD : HEP87_12390 HEP87_40735
SRPZ : HEP85_08070 HEP85_31250
SABD : N8I86_08150 N8I86_29770
SCT : SCAT_0884(rnaSA) SCAT_5357(rnaSA)
SCY : SCATT_08850 SCATT_53540
KAU : B6264_17650 B6264_27575
KIT : CFP65_2288 CFP65_6914
AGLA : OIE69_11110 OIE69_32330
LMOI : VV02_10050 VV02_25570
NOO : FE634_13695 FE634_18880
KSL : OG809_05460 OG809_27315
SACG : FDZ84_05545 FDZ84_19225
AMQ : AMETH_1561 AMETH_1876
AAB : A4R43_18780 A4R43_39475
AMYY : YIM_11015 YIM_38380(rnaSA)
SESP : BN6_14700 BN6_71570
KAL : KALB_1670 KALB_7357 KALB_7358
KPHY : AOZ06_11885 AOZ06_45075
PMAD : BAY61_06610 BAY61_09000
SACE : GIY23_06690 GIY23_17460
» show all
Taxonomy
Reference
1
Authors
Takahashi K.
Title
The structure and function of ribonuclease T1. I. Chromatographic purification and properties of ribonuclease T1.
Journal
J Biochem (Tokyo) 49:1-8 (1961)
Reference
Authors
Kasai K, Uchida T, Egami F, Yoshida K, Nomoto M.
Title
Purification and crystallization of ribonuclease N1 from Neurospora crassa.
Journal
Reference
Authors
Loverix S, Laus G, Martins JC, Wyns L, Steyaert J
Title
Reconsidering the energetics of ribonuclease catalysed RNA hydrolysis.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 4.6.1.24
ExPASy - ENZYME nomenclature database: 4.6.1.24
LinkDB
All DBs