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Literature summary extracted from

  • Zhou, X.; Chua, T.K.; Tkaczuk, K.L.; Bujnicki, J.M.; Sivaraman, J.
    The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket (2010), J. Struct. Biol., 169, 277-285.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.16 expressed as a His-tagged fusion protein Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.16 using the hanging-drop vapour diffusion method. SpeE crystals diffract up to 2.9 A resolution using the Quantum 4-CCD detector. SpeE consists of two domains a small N-terminal beta-strand domain, and a C-terminal catalytic domain that adopts a canonical methyltransferase (MTase) Rossmann fold. Structural comparison of Escherichia coli SpeE to its homologs reveals that it has a large and unique substrate-binding cleft that may account for its lower amine substrate specificity Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.16 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.16 using Ni-NTA chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.16 S-adenosylmethioninamine + putrescine
-
 Escherichia coli 5'-S-methyl-5'-thioadenosine + spermidine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.16 dimer protein forms a dimer in crystal and solution Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.5.1.16 SpeE
-
 Escherichia coli
2.5.1.16 spermidine synthase
-
 Escherichia coli