Species: Haloarcula vallismortis
Subunit composition of glyceraldehyde 3-phosphate dehydrogenase = [glyceraldehyde 3-phosphate dehydrogenase subunit]4
The native molecular mass was estimated by gel filtration chromatography in the presence of 2 molar salt [Pruss93]. The enzyme from this species was determined to be more similar in amino acid sequence to eukaryotes and eubacteria than to enzymes of other archaebacteria [Pruss93].
The subunit relative molecular mass was determined by CTAB-PAGE. This technique is preferable to SDS-PAGE for halophilic proteins [Pruss93].
Molecular Weight of Polypeptide: 38 kD (experimental) [Pruss93 ]
Molecular Weight of Multimer: 160 kD (experimental) [Pruss93]
pI: 4.25 [Pruss93]
Enzymatic reaction of: glyceraldehyde 3-phosphate dehydrogenase
EC Number: 18.104.22.168D-glyceraldehyde 3-phosphate + NAD+ + phosphate ⇄ 1,3-bisphospho-D-glycerate + NADH + H+
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
This reaction is reversible.
The enzyme was shown to be strictly NAD+-dependent and its activity was highest in the presence of 2-3 molar potassium chloride. Arsenate was an alternate substrate for phosphate [Pruss93].
pH(opt): 8.6 [Krishnan90]
Krishnan90: Krishnan G, Altekar W (1990). "Characterization of a halophilic glyceraldehyde-3-phosphate dehydrogenase from the archaebacterium Haloarcula vallismortis." J. Gen. Appl. Microbiol. 36:19-32.
Pruss93: Pruss B, Meyer HE, Holldorf AW (1993). "Characterization of the glyceraldehyde 3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis." Arch Microbiol 160(1);5-11. PMID: 8352651
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