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Literature summary for 1.2.1.12 extracted from

  • Shen, H.; Wang, H.; Liu, Q.; Liu, H.; Teng, M.; Li, X.
    Structural insights into RNA recognition properties of glyceraldehyde-3-phosphate dehydrogenase 3 from Saccharomyces cerevisiae (2014), IUBMB Life, 66, 631-638 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified apo-form GAPDH3, by vapor-diffusing method, mixing 10 mg/mL protein with a reservoir solution containing 12% (w/v) PEG 3350, 0.1 M sodium malonate, pH 4.0, 2 days, at 14°C, X-ray diffraction structure determination and analysis at 2.49 A resolution, modeling Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
NAD+ NAD+ inhibition for GAPDH3 RNA binding capability, NAD+ inhibits the AUUUA binding. The inhibition effect is weaker for the 5-base substrate than for the 13-base substrate. RNA substrate binding needs to competitively displace the NAD+ molecules from the binding groove Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00359
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Saccharomyces cerevisiae 3-phospho-D-glyceroyl phosphate + NADH + H+
-
?

Subunits

Subunits Comment Organism
homotetramer SDS-PAGE and gel filtration Saccharomyces cerevisiae
More quarternary structure analysis and comparisons, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
GAPDH
-
Saccharomyces cerevisiae
GAPDH3
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Saccharomyces cerevisiae
glyceraldehyde-3-phosphate dehydrogenase
-
Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+ binding structure analysis: the NAD+ molecule inserts its pyrimidine ring into a narrow hydrophobic binding pocket on the positively charged surface of GAPDH3. The residues Asn7, Gly8, Phe9, Gly10, Asp33, Pro34, Phe35, The97, Gly98, and Phe100 tightly enclose the pyrimidine ring of NAD+. Because of a common adenine head, adenosine can also bind tightly to this hydrophobic binding pocket. There are two consecutive positively charged regions that contain an NAD+-binding site, one of which is located on each side of the tetramer Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function glyceraldehyde-3-phosphate dehydrogenase is an essential enzyme in the glycolytic pathway. GAPDH also displays a range of other functions unrelated to its glycolytic function. GAPDH is a 3'-AU-rich element-binding protein, it can selectively bind to AU-rich +element, RNA recognition mechanism, overview. NAD1 inhibition for GAPDH3 RNA binding capability indicates that GAPDH3 likely binds to the AU-rich or polyadenosine RNA substrates through its NAD+-binding domain in vitro Saccharomyces cerevisiae