2.5.1.22: spermine synthase

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For detailed information about spermine synthase, go to the full flat file.

Reaction

Synonyms

ACL5, aminopropyltransferase, spermidine, OsSPMS1, SMS, spermidine aminopropyltransferase, spermine synthase, spermine synthase 1, spermine synthetase, Spm synthase, SpmS, SPMS1, SpmSyn, synthase, spermine

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.22 spermine synthase

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Results	in table
1	Activating Compound
42	AA Sequence
5	Application
1	CAS Registry Number
12	Cloned(Commentary)
2	Cofactor
3	Crystallization (Commentary)
122	Disease/ Diagnostics
5	Expression
14	General Information
1	General Stability
4	IC50 Value
66	Inhibitors
7	Ki Value [mM]
23	KM Value [mM]
8	Localization
2	Metals/Ions
10	Molecular Weight [Da]
15	Natural Substrates/ Products (Substrates)
550	Organism
8	Pathway
14	PDB ID
6	pH Optimum
36	Protein Variants
11	Purification (Commentary)
2	Reaction
2	Reaction Type
56	Reference
65	Source Tissue
14	Specific Activity [micromol/min/mg]
1	Storage Stability
51	Substrates and Products (Substrate)
15	Subunits
37	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
10	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.5.1.22 - spermine synthase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

analysis of X-ray crystal structure of the wild-type human SMS in complex with spermidine and 5-methylthioadenosine, PDB ID 3C6K, and folding free energy calculations, dimer structure analysis of wild-type and mutant enzymes, overview

Homo sapiens

P52788

723531

in complex with 5'-methylthioadenosine and spermidine and with 5'-methylthioadenosine and spermine. Enzyme is a dimer of two identical subunits. Each monomer has three domains, a C-terminal domain, which contains the active site and is similar in structure to spermidine synthase, a central domain made up of four beta-strands, and an N-terminal domain with remarkable structural similarity to S-adenosylmethionine decarboxylase

Homo sapiens

P52788

687717

Purified SpmSyn is crystallized as ternary complex in the presence of spermidine and 5'-methylthioadenosine or spermidine and 5'-methylthioadenosine using the hanging drop vapor diffusion method. The SpmSyn-5'-methylthioadenosine-spermidine complex is crystallized in 12% polyethylene glycol and 0.1 M MES (pH 6.5). The SpmSyn-5'-methylthioadenosine-spermine complex is crystallized in 18% polyethylene glycol, 0.1 M NaCl, and 0.1 M BisTris (pH 6.5). Crystals are soaked in the corresponding mother liquor supplemented with 20% glycerol as cryoprotectant before freezing in liquid nitrogen.

Homo sapiens

P52788

692270