Literature summary for 1.1.1.6 extracted from

Zhang, J.; Nanjaraj Urs, A.N.; Lin, L.; Zhou, Y.; Hu, Y.; Hua, G.; Gao, Q.; Yuchi, Z.; Zhang, Y.
Structure of glycerol dehydrogenase (GldA) from Escherichia coli (2019), Acta Crystallogr. Sect. F, 75, 176-183 .

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapor-diffusion method at 22°C, solved at 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 3(10)-helices and several loops organized into two domains, the N- and C-terminal domains. The active site is located in a deep cleft between the two domains	Escherichia coli
structure containing glycerol in the active site, to 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 310-helices and several loops organized into the N- and C-terminal domains. The active site is located in a deep cleft between the two domains. The N-terminal domain contains a classic Rossmann fold for NAD+ binding. The glycerol molecule is sandwiched by the Zn2+ and NAD+ ions	Escherichia coli

Crystallization (Comment)

Organism

sitting-drop vapor-diffusion method at 22°C, solved at 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 3(10)-helices and several loops organized into two domains, the N- and C-terminal domains. The active site is located in a deep cleft between the two domains

Escherichia coli

structure containing glycerol in the active site, to 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 310-helices and several loops organized into the N- and C-terminal domains. The active site is located in a deep cleft between the two domains. The N-terminal domain contains a classic Rossmann fold for NAD+ binding. The glycerol molecule is sandwiched by the Zn2+ and NAD+ ions

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the glycerol molecule is sandwiched by the Zn2+ and NAD+ ions	Escherichia coli
Zn2+	computer modeling suggests that the glycerol molecule is sandwiched by the Zn2+ and NAD+ ions	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
161000	-	-	Escherichia coli
161000	-	gel filtration	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9S5	-	-
Escherichia coli	P0A9S5	substrain MG1655	-
Escherichia coli K12	P0A9S5	substrain MG1655	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli
recombinant protein, purified to homogeneity using a combination of heat-shock and chromatographic methods	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
glycerol + NAD+	-	Escherichia coli	glycerone + NADH + H+	-	?
glycerol + NAD+	-	Escherichia coli K12	glycerone + NADH + H+	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 39000, SDS-PAGE	Escherichia coli

Synonyms

Synonyms	Comment	Organism
GldA	-	Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
65.6	-	melting temperature	Escherichia coli
65.6	-	Tm-value	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	the enzyme is required to catalyze the first step in fermentative glycerol metabolism	Escherichia coli