Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
class II aldolase/adducin family protein
This family includes class II aldolases and adducins which have not been ascribed any enzymatic function. [1]. 8515438. The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli. Dreyer MK, Schulz GE;. J Mol Biol 1993;231:549-553. [2]. 8676381. Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. Dreyer MK, Schulz GE;. J Mol Biol 1996;259:458-466. (from Pfam)
L-fuculose-phosphate aldolase
L-fuculose-phosphate aldolase catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde; Also able to catalyze the reversible cleavage of D-ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1-phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively
Catalyzes the formation of glycerone phosphate and (S)-lactaldehyde from L-fuculose 1-phosphate
Members of this family are L-fuculose phosphate aldolase from various Proteobacteria, encoded in fucose utilization operons. Homologs in other bacteria given similar annotation but scoring below the trusted cutoff may share extensive sequence similarity but are not experimenally characterized and are not found in apparent fucose utilization operons; we consider their annotation as L-fuculose phosphate aldolase to be tenuous. This model has been narrowed in scope from the previous version.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on