KEGG   ENZYME: 2.5.1.44Help
Entry
EC 2.5.1.44                 Enzyme                                 

Name
homospermidine 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)
BRITE hierarchy
Sysname
putrescine:putrescine 4-aminobutyltransferase (ammonia-forming)
Reaction(IUBMB)
(1) 2 putrescine = sym-homospermidine + NH3 + H+ [RN:R00018];
(2) putrescine + spermidine = sym-homospermidine + propane-1,3-diamine [RN:R01919]
Reaction(KEGG)
Substrate
putrescine [CPD:C00134];
spermidine [CPD:C00315]
Product
sym-homospermidine [CPD:C06366];
NH3 [CPD:C00014];
H+ [CPD:C00080];
propane-1,3-diamine [CPD:C00986]
Comment
The reaction of this enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: NAD+-dependent dehydrogenation of putrescine, transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine and reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. Differs from EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group.
Pathway
Tropane, piperidine and pyridine alkaloid biosynthesis
Biosynthesis of secondary metabolites
Orthology
K00808  
homospermidine synthase
Genes
PAU: 
PAP: 
PDK: 
PST: 
SAZ: 
AMAA: 
LPN: 
lpg2495(hss)
LPU: 
LPF: 
LPP: 
LPC: 
LPA: 
LPE: 
LLO: 
REH: 
CTI: 
BGE: 
VAP: 
NEU: 
NE1498(hss)
NII: 
NMU: 
MLO: 
MCI: 
MOP: 
MAM: 
MES: 
PLA: 
SME: 
SMK: 
SMQ: 
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SMEG: 
SMEL: 
SMD: 
RHI: 
SFH: 
SFD: 
ATU: 
ARA: 
AVI: 
AGR: 
RET: 
REC: 
RLE: 
RL4073(hss)
RLT: 
RLG: 
RTR: 
BME: 
BMZ: 
BMG: 
BMW: 
BMF: 
BMB: 
BMC: 
BAA: 
BMS: 
BSI: 
BMT: 
BSV: 
BOV: 
BCS: 
BSK: 
BMR: 
BPP: 
OAN: 
BJA: 
BJU: 
BRA: 
BBT: 
BRS: 
RPA: 
RPB: 
RPC: 
RPD: 
RPE: 
RPT: 
RPX: 
NWI: 
NHA: 
OCA: 
OCG: 
OCO: 
AOL: 
XAU: 
AZC: 
SNO: 
MEX: 
MEA: 
MDI: 
MCH: 
MRD: 
MET: 
MPO: 
MNO: 
BID: 
MSL: 
MSC: 
JAN: 
DSH: 
GBE: 
RCE: 
MAG: 
AZL: 
ALI: 
ABS: 
TMO: 
PGV: 
MAI: 
MAN: 
TPX: 
OTE: 
CALO: 
PPH: 
MAC: 
MBA: 
MMA: 
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MBN: 
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 » show all
Taxonomy
Reference
1  [PMID:437275]
  Authors
Tait GH.
  Title
The formation of homospermidine by an enzyme from Rhodopseudomonas viridis [proceedings]
  Journal
Biochem. Soc. Trans. 7 (1979) 199-201.
  Organism
Rhodopseudomonas viridis
Reference
2
  Authors
Bottcher, F., Ober, D. and Hartmann, T.
  Title
Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation.
  Journal
Can. J. Chem. 72 (1994) 80-85.
Reference
3  [PMID:8407874]
  Authors
Yamamoto S, Nagata S, Kusaba K.
  Title
Purification and characterization of homospermidine synthase in Acinetobacter tartarogenes ATCC 31105.
  Journal
J. Biochem. (Tokyo). 114 (1993) 45-9.
  Organism
Acinetobacter tartarogenes
Reference
4  [PMID:7470060]
  Authors
Srivenugopal KS, Adiga PR.
  Title
Enzymic synthesis of sym-homospermidine in Lathyrus sativus (grass pea) seedlings.
  Journal
Biochem. J. 190 (1980) 461-4.
  Organism
Lathyrus sativus
Reference
5
  Authors
Ober, D., Tholl, D., Martin, W. and Hartmann, T.
  Title
Homospermidine synthase of Rhodopseudomonas viridis: Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichia coli.
  Journal
J. Gen. Appl. Microbiol. 42 (1996) 411-419.
Reference
6  [PMID:10611289]
  Authors
Ober D, Hartmann T.
  Title
Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 14777-82.
  Organism
Senecio vernalis
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
76106-84-8

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