KEGG   ENZYME: 3.5.3.24
Entry
EC 3.5.3.24                 Enzyme                                 
Name
N1-aminopropylagmatine ureohydrolase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amidines
Sysname
N1-(aminopropyl)agmatine amidinohydrolase
Reaction(IUBMB)
N1-(aminopropyl)agmatine + H2O = spermidine + urea [RN:R10347]
Reaction(KEGG)
R10347
Substrate
N1-(aminopropyl)agmatine [CPD:C20560];
H2O [CPD:C00001]
Product
spermidine [CPD:C00315];
urea [CPD:C00086]
Comment
The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.
History
EC 3.5.3.24 created 2013
Reference
1  [PMID:15983049]
  Authors
Ohnuma M, Terui Y, Tamakoshi M, Mitome H, Niitsu M, Samejima K, Kawashima E, Oshima T
  Title
N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus.
  Journal
J Biol Chem 280:30073-82 (2005)
DOI:10.1074/jbc.M413332200
  Sequence
[tth:TT_C0764]
Reference
2  [PMID:20675472]
  Authors
Morimoto N, Fukuda W, Nakajima N, Masuda T, Terui Y, Kanai T, Oshima T, Imanaka T, Fujiwara S
  Title
Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis.
  Journal
J Bacteriol 192:4991-5001 (2010)
DOI:10.1128/JB.00279-10
  Sequence
[tko:TK0882]
Other DBs
ExplorEnz - The Enzyme Database: 3.5.3.24
IUBMB Enzyme Nomenclature: 3.5.3.24
ExPASy - ENZYME nomenclature database: 3.5.3.24
BRENDA, the Enzyme Database: 3.5.3.24

  All links  
Chemical substance (4)   
   KEGG COMPOUND (4)   
Chemical reaction (3)   
   KEGG REACTION (1)   
   KEGG RCLASS (2)   
Protein sequence (184)   
   UniProt (181)   
   SWISS-PROT (3)   
DNA sequence (94)   
   GenBank (47)   
   EMBL (47)   
Protein domain (3)   
   InterPro (3)   
All databases (288)   

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