5YAT

Crystal structure of mitochondrial alcohol dehydrogenase isozyme III from Komagataella phaffii GS115

Summary for 5YAT

• Entry DOI: 10.2210/pdb5yat/pdb
• Descriptor: Mitochondrial alcohol dehydrogenase isozyme III, GLYCEROL, ISOPROPYL ALCOHOL, ... (5 entities in total)
• Functional Keywords: alcohol dehydrogenase, catalytic zinc, yeast, dimer, oxidoreductase
• Biological source: Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast)
• Total number of polymer chains: 2
• Total formula weight: 74826.55

Authors

Zhang, H.D.,Li, Q. (deposition date: 2017-09-01, release date: 2018-03-21, Last modification date: 2023-11-22)

Primary citation

Zhang, H.,Li, Q.,Wang, L.,Chen, Y.
Investigation of structure and function of mitochondrial alcohol dehydrogenase isozyme III from Komagataella phaffii GS115.
Biochim. Biophys. Acta, 1862:1199-1208, 2018

PubMed Abstract: Alcohol dehydrogenases (ADHs) catalyze the reversible oxidation of alcohol using NAD or NADP as cofactor. Three ADH homologues have been identified in Komagataella phaffii GS115 (also named Pichia pastoris GS115), ADH1, ADH2 and ADH3, among which adh3 is the only gene responsible for consumption of ethanol in Komagataella phaffii GS115. However, the relationship between structure and function of mitochondrial alcohol dehydrogenase isozyme III from Komagataella phaffii GS115 (KpADH3) is still not clear yet.

PubMed: 29474823
DOI: 10.1016/j.bbagen.2018.02.012

Experimental method

X-RAY DIFFRACTION (1.745 Å)