Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.16 - spermidine synthase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC2.5.1.16
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
spermidine synthase, aminopropyltransferase, spds2, spdsyn, spd synthase, mdspds1, spermidine synthase 1, pgspd, putrescine aminopropyltransferase, spermidine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopropyltransferase
-
-
-
-
aminopropyltransferase spermidine synthase
-
-
-
-
putrescine aminopropyltransferase
-
-
-
-
spermidine synthetase
-
-
-
-
synthase, spermidine
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
single displacement reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopropyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase
The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
CAS REGISTRY NUMBER
COMMENTARY hide
37277-82-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
show the reaction diagram
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cyclohexylamine
-
potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
S-Adenosyl-1,8-diamino-3-thiooctane
-
competitive with 1,4-diaminobutane, potent inhibition, stronger than dicyclohexylamine in vitro, but not in vivo, at concentrations of S-adenosyl-3-methylthio-1-propylamine and 1,4-diaminobutane higher than those normally present in vivo. At concentration of substrates that approximate in vivo conditions, more than 20fold stronger inhibition
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A2R3J1G4_PSEAI
375
0
42287
TrEMBL
-
A0A2R3J0J3_PSEAI
248
0
27508
TrEMBL
-
A0A3M5DU97_PSEAI
298
0
33836
TrEMBL
-
A0A8G7JZL6_PSEAI
349
0
39601
TrEMBL
-
A0A485GS88_PSEAI
376
0
42404
TrEMBL
-
A0A8F9JSM5_PSEAI
375
0
42281
TrEMBL
-
A0A8F9IWY7_PSEAI
299
0
33963
TrEMBL
-
A0A8G2XH29_PSEAI
286
0
32243
TrEMBL
-
A0A8G3W4M1_PSEAI
349
0
39519
TrEMBL
-
A0A8B5B2P5_PSEAI
341
0
38838
TrEMBL
-
A0A431XBF0_PSEAI
349
0
39479
TrEMBL
-
A0A8G6CVI9_PSEAI
349
0
39501
TrEMBL
-
A0A8G7I2R4_PSEAI
349
0
39501
TrEMBL
-
A0A8G4D6S4_PSEAI
286
0
32229
TrEMBL
-
A0A8G4N6G2_PSEAI
286
0
32270
TrEMBL
-
A0A8G2TNK3_PSEAI
286
0
32268
TrEMBL
-
A0A0A8RHJ2_PSEAI
375
0
42297
TrEMBL
-
A0A0C6EWL7_PSEAI
286
0
32257
TrEMBL
-
A0A0F6UEF8_PSEAI
286
0
32199
TrEMBL
-
A0A8G6GZL4_PSEAI
286
0
32256
TrEMBL
-
A0A485G3C0_PSEAI
434
0
49116
TrEMBL
-
A0A8G4NMD9_PSEAI
349
0
39573
TrEMBL
-
A0A8G6T7S4_PSEAI
286
0
32311
TrEMBL
-
A0A8B4ZI25_PSEAI
286
0
32238
TrEMBL
-
A0A2R3IRB0_PSEAI
286
0
32164
TrEMBL
-
A0A0A8RPN0_PSEAI
336
0
37797
TrEMBL
-
A0A8G8ETJ6_PSEAI
349
0
39533
TrEMBL
-
A0A8F9VHK1_PSEAI
375
0
42339
TrEMBL
-
A0A7M3B3V9_PSEAI
349
0
39503
TrEMBL
-
A0A431XG60_PSEAI
286
0
32194
TrEMBL
-
A0A0D6H8P6_PSEAI
248
0
27758
TrEMBL
-
A0A8G3UB73_PSEAI
349
0
39575
TrEMBL
-
A0A8B5A083_PSEAI
349
0
39517
TrEMBL
-
A0A8G2RX85_PSEAI
286
0
32286
TrEMBL
-
A0A8G5UJT5_PSEAI
349
0
39546
TrEMBL
-
A0A8F9NTI9_PSEAI
286
0
32287
TrEMBL
-
A0A8G1VCH1_PSEAI
375
0
42267
TrEMBL
-
A0A8G4M606_PSEAI
349
0
39519
TrEMBL
-
A0A643ED69_PSEAI
349
0
39595
TrEMBL
-
A0A8G5J7H6_PSEAI
349
0
39563
TrEMBL
-
A0A8G7TFP2_PSEAI
349
0
39519
TrEMBL
-
A0A8G1VFX1_PSEAI
286
0
32287
TrEMBL
-
A0A8G6ZNT5_PSEAI
349
0
39562
TrEMBL
-
A0A241XXR3_PSEAI
349
0
39517
TrEMBL
-
A0A2V3EZ72_PSEAI
349
0
39547
TrEMBL
-
A0A8G2NFS6_PSEAI
349
0
39574
TrEMBL
-
A0A8G4NNX1_PSEAI
349
0
39543
TrEMBL
-
A0A6M3UXB5_PSEAI
375
0
42253
TrEMBL
-
A0A8G1K6T0_PSEAI
375
0
42297
TrEMBL
-
A0A8I0ZKD8_PSEAI
375
0
42311
TrEMBL
-
A0A8F9Y680_PSEAI
286
0
32275
TrEMBL
-
A0A8G7IMA6_PSEAI
349
0
39545
TrEMBL
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pegg, A.E.; Bitonti, A.J.; McCann, P.P.; Coward, J.K.
Inhibition of bacterial aminopropyltransferases by S-adenosyl-1,8-diamino-3-thiooctane and by dicyclohexylamine
FEBS Lett.
155
192-196
1983
Escherichia coli, Pseudomonas aeruginosa, Rattus norvegicus, Serratia marcescens
Manually annotated by BRENDA team