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Literature summary for 4.1.2.4 extracted from

  • Cao, T.P.; Kim, J.S.; Woo, M.H.; Choi, J.M.; Jun, Y.; Lee, K.H.; Lee, S.H.
    Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis (2016), J. Microbiol., 54, 311-321 .
    View publication on PubMed
Search for more literature for 4.1.2.4

Cloned(Commentary)

Cloned (Comment) Organism
-
 Streptococcus suis

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, crystal structures of full length and C-terminal truncated enzyme is determined at 2.8 A resolution. Both contain the typical (alpha/beta)8 TIM-barrel fold of class I aldolases. C-terminal truncation resulting in missing the last alpha9 and beta8 secondary elements, allows the enzyme to maintain activity comparable to the full length enzyme. Arg186 and Ser205 residues at the C-terminus appear mutually supplemental or less indispensible for substrate phosphate moiety recognition Streptococcus suis

Organism

Organism UniProt Comment Textmining
Streptococcus suis D5AHU8
-
-
Streptococcus suis GZ1 D5AHU8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptococcus suis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-ribose 5-phosphate
-
 Streptococcus suis D-glyceraldehyde 3-phosphate + acetaldehyde
-
 ?
2-deoxy-D-ribose 5-phosphate
-
 Streptococcus suis GZ1 D-glyceraldehyde 3-phosphate + acetaldehyde
-
 ?

Synonyms

Synonyms Comment Organism
2-Deoxyribose-5-phosphate aldolase
-
 Streptococcus suis
DERA
-
 Streptococcus suis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Streptococcus suis