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Literature summary for 2.2.1.2 extracted from

  • Huang, H.; Rong, H.; Li, X.; Tong, S.; Zhu, Z.; Niu, L.; Teng, M.
    The crystal structure and identification of NQM1/YGRO43C, a transaldolase from Saccharomyces cerevisiae (2008), Proteins Struct. Funct. Genet., 73, 1076-1081.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53228
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+ affinity column Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 6-phosphate + erythrose 4-phosphate assay at pH 7.6 Saccharomyces cerevisiae sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
-
 ?

Synonyms

Synonyms Comment Organism
NQM1/YGR043C
-
 Saccharomyces cerevisiae
transaldolase
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction dysfunction could lead to liver cirrhosis and neonatal multi-organ diseases Saccharomyces cerevisiae
physiological function key enzyme in pentose phosphate pathway Saccharomyces cerevisiae