Literature summary extracted from

Roychoudhury, S.; Chakrabarty, K.; Ho, Y.K.; Chakrabarty, A.M.
Characterization of guanosine diphospho-D-mannose dehydrogenase from Pseudomonas aeruginosa. Structural analysis by limited proteolyses (1992), J. Biol. Chem., 267, 990-996.

General Stability

EC Number	General Stability	Organism
1.1.1.132	repeated freezing/thawing leads to decrease of activity	Pseudomonas aeruginosa

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.1.1.132	GMP	-	Pseudomonas aeruginosa

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.1.1.132	48000	-	SDS-PAGE	Pseudomonas aeruginosa

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.132	Pseudomonas aeruginosa	-	algD gene overproduced in strain 8822 using a plasmid vector containing algD under control of the tac promoter	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
1.1.1.132	GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH + 2 H+	class of 4-electron transfer dehydrogenases	Pseudomonas aeruginosa	a

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.1.1.132	additional information	-	presence of 1 mM GDP-mannose, GDP-glucose, GMP, GDP, GTP or cGMP retards tryptic digest of enzyme and protects subsequent loss of enzyme activity, amino-terminal domain contains substrate and cofactor binding sites, carboxy-terminal domain is essential for catalytic activity	Pseudomonas aeruginosa

Storage Stability

EC Number	Storage Stability	Organism
1.1.1.132	-70°C, 1-3 mg/ml purified protein, 50 mM triethanolamine acetate, pH 7.6, 1 mM DTT	Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.132	GDP-mannose + NAD+ + H2O	-	Pseudomonas aeruginosa	GDP-mannuronate + NADH	-	?

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.1.1.132	NAD+	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)