speH (S-adenosylmethionine decarboxylase proenzyme)
FEATURES
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ORGANISM
Hungateiclostridium thermocellum (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
FAMILY
DESCRIPTION
Also known as SPEH_HUNT2, speH. Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Also known as SPEH_HUNT2, speH. Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
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speH

S-adenosylmethionine decarboxylase proenzyme

Molecular Synopsis