Literature summary for 1.2.1.79 extracted from

Ahn, J.-W.; Kim, Y.-G.; Kim, K.-J.
Crystal structure of non-redox regulated SSADH from Escherichia coli (2010), Biochem. Biophys. Res. Commun., 392, 106-111.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.4 A resolution. The overall structure of SSADH shares the general fold of ALDH classes 1 and 2. The SSADH monomer is composed of three domains; an N-terminal NAD(P)-binding domain of residues 1125, 148256, and 457472, a catalytic domain of residues 257456, and an oligomerization domain of residues 126147 and 473482. The catalytic loop of Escherichia coli SSADH, unlike that of human SSADH, does not undergo disulfide bond-mediated structural changes upon changes of environmental redox status. The protein is not regulated via redox-switch modulation. A difference in the conformation of the connecting loop beta15beta16 causes the formation of a water molecule-mediated hydrogen bond network between the connecting loop and the catalytic loop in Escherichia coli SSADH	Escherichia coli

Crystallization (Comment)

Organism

to 1.4 A resolution. The overall structure of SSADH shares the general fold of ALDH classes 1 and 2. The SSADH monomer is composed of three domains; an N-terminal NAD(P)-binding domain of residues 1125, 148256, and 457472, a catalytic domain of residues 257456, and an oligomerization domain of residues 126147 and 473482. The catalytic loop of Escherichia coli SSADH, unlike that of human SSADH, does not undergo disulfide bond-mediated structural changes upon changes of environmental redox status. The protein is not regulated via redox-switch modulation. A difference in the conformation of the connecting loop beta15beta16 causes the formation of a water molecule-mediated hydrogen bond network between the connecting loop and the catalytic loop in Escherichia coli SSADH

Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Escherichia coli	5829	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)