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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.2 Saccharomyces cerevisiae P53228
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.2.1.2 Ni2+ affinity column Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.2.1.2 3.4
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.2.1.2 NQM1/YGR043C
-
 Saccharomyces cerevisiae
2.2.1.2 transaldolase
-
 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.2.1.2 7.6
-
 assay at Saccharomyces cerevisiae

General Information

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