KEGG   ENZYME: 2.5.1.128
Entry
EC 2.5.1.128                Enzyme                                 
Name
N4-bis(aminopropyl)spermidine synthase
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)
Sysname
S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase [N4-bis(aminopropyl)spermidine synthesizing]
Reaction(IUBMB)
2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 S-methyl-5'-thioadenosine + N4-bis(aminopropyl)spermidine (overall reaction) [RN:R11154];
(1a) S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5'-thioadenosine + N4-aminopropylspermidine [RN:R11159];
(1b) S-adenosyl 3-(methylsulfanyl)propylamine + N4-aminopropylspermidine = S-methyl-5'-thioadenosine + N4-bis(aminopropyl)spermidine [RN:R11160]
Reaction(KEGG)
Substrate
S-adenosyl 3-(methylsulfanyl)propylamine [CPD:C01137];
spermidine [CPD:C00315];
N4-aminopropylspermidine [CPD:C21009]
Product
S-methyl-5'-thioadenosine [CPD:C00170];
N4-bis(aminopropyl)spermidine [CPD:C21010];
N4-aminopropylspermidine [CPD:C21009]
Comment
The enzyme, characterized from the thermophilic archaeon Thermococcus kodakarensis, synthesizes the branched-chain polyamine N4-bis(aminopropyl)spermidine, which is required for cell growth at high-temperature. When spermine is used as substrate, the enzyme forms N4-aminopropylspermine.
History
EC 2.5.1.128 created 2014
Orthology
K07057  N4-bis(aminopropyl)spermidine synthase
Genes
GTKGT3570_09820
GGHGHH_c21380
GEAGARCT_00701
GSRGS3922_12390
GZAIC807_06460
PTBDER53_08120
CTHUHUR95_08205
HYIK2M58_02480
PABSJIR001_06140 JIR001_09810
DKUDesku_2563
TTETTE1898
TEXTeth514_1121
THXThet_1792
TPDTeth39_0634
TITThit_1686
TMTTmath_1670
TBOThebr_0649
TWIThewi_1855
TKITKV_c17620
CHYCHY_0365
ADGAdeg_0209
CSCCsac_1231
ATEAthe_2198
COBCOB47_1979
CHDCalhy_0562
COWCalow_1887
CKICalkr_0377
CLCCalla_1981
CKNCalkro_0440
CCHAELD05_03145
CDIACaldiYA01_03930
TOCToce_1644
THUGKNN16_00465(speD)
TTHTT_C0171
TTJTTHA0539(TTHA0539)
TTSThthe16_0538
TTLTtJL18_1537
TPARAV541_07995
TLITlie_1345
AMOAnamo_0349
RMRRmar_0533
RMGRhom172_0537
AAEaq_1754
HYAHY04AAS1_0834
HHOHydHO_0829
HYSHydSN_0847
HTHHTH_1277
HTEHydth_1269
TALThal_1053
TRDTHERU_06865
SULSYO3AOP1_0154
SAFSULAZ_0710
PMXPERMA_1439
TTKTST_0020
TAMTheam_0292
DTEDester_0229
TTATheth_1513
CPOCOPRO5265_0690
CEXCSE_05650
TIDThein_2228
TOPTOPB45_1193
TCMHL41_00370
THETF1847_06500
CTHITHC_1142
TAVG4V39_04970
TMAIFVE67_06940
BANABARAN1_0480(bpsA)
BIHBIP78_1087
MJAMJ_0675 MJ_1273
MFEMefer_0046 Mefer_0624
MVUMetvu_0675 Metvu_0723
MFSMFS40622_0658 MFS40622_1505
MIFMetin_0014 Metin_1435
MJHJH146_0452 JH146_1223
MESGMLAUSG7_0027(bpsA) MLAUSG7_0362
MESAMLASG1_1207(bpsA) MLASG1_1541
MIGMetig_0730 Metig_0858
MMPMMP1657
MMQMmarC5_1752
MMXMmarC6_1016
MMZMmarC7_0929
MMDGYY_09140
MMAKMMKA1_18890
MMAOMMOS7_17700
MMADMMJJ_11750(bpsA)
MAEMaeo_0142
MVNMevan_0957
MVOMvol_1306
MOKMetok_0901
METFCFE53_00405 CFE53_00505
AFUAF_1611
AFGAFULGI_00018620
APOArcpr_0370
AVEArcve_0369
ASTAsulf_00865
FPLFerp_1880
GACGACE_1398
GAHGAH_01086
PFUPF1111
PFIPFC_04775
PHOPH0728(PH0728)
PABPAB0872
PYNPNA2_1371
PYAPYCH_02980
PYSPy04_0736
PYCTQ32_03155
TKOTK1691
TONTON_1358
TGATGAM_0371
TSITSIB_0126
TBATERMP_01367
THEGQS_08760
THATAM4_1077
THMCL1_1351
TLTOCC_06976
THSTES1_1386
TNUBD01_1992
TEUTEU_04560
TGYX802_05695
THVADU37_CDS00470
TCHCHITON_1122
TPEPA0127_06790
TPIEA7C91_02470
TGGA3K92_06945
TCEA3L02_04365
TBSA3L01_07525
THHCDI07_08060
TSLA3L11_00505
TTDA3L14_09890
TPRFA3L09_00360
TRLA3L10_06925
TPAFA3L08_00720
THYA3L12_01265
TICFH039_10455
TCQTIRI35C_1826(bpsA)
THEMFPV09_10415
THEIK1720_03715
PPACPAP_09495
ABIAboo_0499
ACFAciM339_0545
PSYTDSAG12_02754
 » show all
Reference
1  [PMID:24610711]
  Authors
Okada K, Hidese R, Fukuda W, Niitsu M, Takao K, Horai Y, Umezawa N, Higuchi T, Oshima T, Yoshikawa Y, Imanaka T, Fujiwara S
  Title
Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles.
  Journal
J Bacteriol 196:1866-76 (2014)
DOI:10.1128/JB.01515-14
  Sequence
[tko:TK1691]
Other DBs
ExplorEnz - The Enzyme Database: 2.5.1.128
IUBMB Enzyme Nomenclature: 2.5.1.128
ExPASy - ENZYME nomenclature database: 2.5.1.128
BRENDA, the Enzyme Database: 2.5.1.128
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