Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism.
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Human spermine synthase is a homodimer of identical subunits; dimerization occurs mainly through the N-terminal domain and deletion of that domain abolishes activity.
"They show that the enzyme is a dimer of two identical subunits."
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The catalytic mechanism relies on conserved acidic residues (Asp201, Asp276, Glu353), confirmed by site-directed mutagenesis.
"Two residues (Asp 201 and Asp 276 ) that are conserved in aminopropyltransferases"
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
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SMS was detected among ~900 proteins in a shotgun proteomic survey of urinary exosome preparations, without functional characterization at that site.
"In pooled EPS-urine exosome samples, ~900 proteins were detected."
Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX.
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SMS (spermine synthase) maps to Xp22.1 (11 exons over 54 kb) and encodes a ubiquitous enzyme of polyamine metabolism.
"spermine synthase (SpS), which encodes a ubiquitous enzyme of polyamine metabolism"
dc-Adenosyl methionine + Spermidine => Spermine + 5'-methylthioadenosine