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Literature summary for 1.2.1.12 extracted from

  • Ismail, S.A.; Park, H.W.
    Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase (2005), Acta Crystallogr. Sect. D, D61, 1508-1513.
    View publication on PubMed
Search for more literature for 1.2.1.12

Application

Application Comment Organism
medicine functions are of chemotherapeutic interest, structure is a necessity for structure-based drug design Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
subcloned into the pET15b vector for expression in Escherichia coli cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
the structure is presented at 2.5 A resolution Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Homo sapiens
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Homo sapiens P04406
-
-

Purification (Commentary)

Purification (Comment) Organism
by affinity chromatography on a Hi-Trap chelating column charged with nickel sulfate, the His tag is cleaved and the enzyme is purified by an additional gel filtration step Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-
skeletal muscle for structural comparison Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Homo sapiens 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r

Subunits

Subunits Comment Organism
homotetramer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
GAPDH
-
 Homo sapiens
glyceraldehyde-3-phosphate dehydrogenase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH each subunit is bound to one NAD+ Homo sapiens