Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

Information on EC 4.1.2.62 - 5-deoxyribulose 1-phosphate aldolase

for references in articles please use BRENDA:EC4.1.2.62

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
IUBMB Comments

The enzyme, originally characterized from the bacterium Rhodospirillum rubrum, is involved in degradation pathways for 5'-deoxyadenosine and S-methyl-5'-thioadenosine, which are formed from S-adenosyl-L-methionine (SAM, AdoMet) by radical SAM enzymes and other types of SAM-dependent enzymes, respectively. The enzyme requires a divalent metal cation, with Co2+ producing the highest activity.

The enzyme appears in viruses and cellular organisms

Synonyms
5-(methylthio)ribulose-1-P aldolase, 5-(methylthio)ribulose-1-phosphate aldolase, 5-deoxyribose disposal aldolase, ald2, DrdA, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-deoxy-D-ribulose 1-phosphate = glycerone phosphate + acetaldehyde
show the reaction diagram
(1)
-
-
-
S-methyl-5-thio-D-ribulose 1-phosphate = glycerone phosphate + (2-methylsulfanyl)acetaldehyde
show the reaction diagram
(2)
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
Highest Expressing Human Cell Lines
Cell Line Links Gene Links