Literature summary for 1.1.1.1 extracted from

Guntupalli, S.R.; Li, Z.; Chang, L.; Plapp, B.V.; Subramanian, R.
Cryo-electron microscopy structures of yeast alcohol dehydrogenase (2021), Biochemistry, 60, 663-677 .

Search for more literature for 1.1.1.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme as apoenzyme, in two different binary complexes with NADH, and in a ternary complex with NAD+ and 2,2,2-trifluoroethanol, X-ray diffraction structure determination and analysis at 2.8-3.8 A resolution, modeling	Saccharomyces pastorianus

Protein Variants

Protein Variants	Comment	Organism
I151V	polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, the removal of the methyl group has only weak effects on the structure of the neighboring residues	Saccharomyces pastorianus
Q127E	polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, not readily distinguishable at the current resolutions, and the local structure is not significantly altered	Saccharomyces pastorianus
Q147E	polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, not readily distinguishable at the current resolutions, and the local structure is not significantly altered	Saccharomyces pastorianus
V58T	polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, not readily distinguishable at the current resolutions, and the local structure is not significantly altered	Saccharomyces pastorianus

Inhibitors

Inhibitors	Comment	Organism	Structure
pyrazole	potent inhibitor, binding to the enzyme-NAD+ complex. The enzyme made with NADH and pyrazole has the closed conformation with NADH bound in the active site and the classical coordination of the zinc with a water	Saccharomyces pastorianus
trifluoroethanol	potent inhibitor, binding to the enzyme-NAD+ complex	Saccharomyces pastorianus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	coordination of the active site zinc, overview. The apoenzyme has an open conformation where the cleft between the coenzyme and catalytic domains allows the coenzyme to bind, and the catalytic zinc has an inverted coordination with Cys43, His66, Cys153, and Glu67, the catalytic zinc is coordinated to Glu67. This structure is similar to those of the apoenzyme forms determined by X-ray crystallography (PDB ID 4W6Z). The complex made with NADH also has an open conformation and the inverted zinc coordination	Saccharomyces pastorianus

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces pastorianus	B6UQD0	Saccharomyces cerevisiae x Saccharomyces eubayanus	-

Purification (Commentary)

Purification (Comment)	Organism
the purified commercial preparation is further purified by gel filtration and ultrafiltration	Saccharomyces pastorianus

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	-	Saccharomyces pastorianus	-

Subunits

Subunits	Comment	Organism
More	enzyme tertiary and quaternary structures analysis, overview. The apoenzyme has an open conformation where the cleft between the coenzyme and catalytic domains allows coenzyme to bind, and the catalytic zinc has an inverted coordination with Cys43, His66, Cys153, and Glu67. This structure is similar to those of the apoenzyme forms determined by X-ray crystallography (PDB ID 4W6Z). The complex made with NADH also has an open conformation and the inverted zinc coordination, and NADH is bound to the coenzyme binding domain in a position similar to that found for NAD+ in the B chain subunit in the X-ray structure (PDB ID 5ENV). In contrast, the structure for the sample of the enzyme made with NADH and pyrazole has the closed conformation with NADH bound in the active site and the classical coordination of the zinc with a water	Saccharomyces pastorianus
tetramer	dimer of dimers, crystal structure analysis by cryo-electron microscopy	Saccharomyces pastorianus

Cofactor

Cofactor	Comment	Organism	Structure
additional information	the apoenzyme has an open conformation where the cleft between the coenzyme and catalytic domains allows coenzyme to bind. This structure is similar to those of the apoenzyme forms determined by X-ray crystallography (PDB ID 4W6Z). The complex made with NADH also has an open conformation and the inverted zinc coordination, and NADH is bound to the coenzyme binding domain in a position similar to that found for NAD+ in the B chain subunit in the X-ray structure (PDB ID 5ENV). In contrast, the structure for the sample of the enzyme made with NADH and pyrazole has the closed conformation with NADH bound in the active site and the classical coordination of the zinc with a water	Saccharomyces pastorianus
NAD+	-	Saccharomyces pastorianus
NADH	three-dimensional enzyme-bound structure analysis	Saccharomyces pastorianus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)