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Literature summary for 2.5.1.79 extracted from

  • Romer, P.; Faltermeier, A.; Mertins, V.; Gedrange, T.; Mai, R.; Proff, P.
    Investigations about N-aminopropyl transferases probably involved in biomineralization (2008), J. Physiol. Pharmacol., 59 Suppl 5, 27-37.
    View publication on PubMed
Search for more literature for 2.5.1.79

Cloned(Commentary)

Cloned (Comment) Organism
expression with His6-tag Thalassiosira pseudonana

Protein Variants

Protein Variants Comment Organism
E156D besides main product thermospermine, mutant is able to synthesize some spermine Thalassiosira pseudonana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.091
-
 S-adenosyl-L-methioninamine
-
 Thalassiosira pseudonana
0.104
-
 spermidine
-
 Thalassiosira pseudonana

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
 4 * 48000, SDS-PAGE Thalassiosira pseudonana
196000
-
 native PAGE Thalassiosira pseudonana

Organism

Organism UniProt Comment Textmining
Thalassiosira pseudonana
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.313
-
 pH 9.4, 55°C Thalassiosira pseudonana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methioninamine + spermidine
-
 Thalassiosira pseudonana 5'-methylthioadenosine + thermospermine sole product ?

Subunits

Subunits Comment Organism
tetramer 4 * 48000, SDS-PAGE Thalassiosira pseudonana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Thalassiosira pseudonana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.4 9.6
-
 Thalassiosira pseudonana