Literature summary extracted from

Hyman, M.R.; Arp, D.J.
An electrophoretic study of the thermal- and reductant-dependent aggregation of the 27 kDa component of ammonia monooxygenase from Nitrosomonas europaea (1993), Electrophoresis, 14, 619-627.

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
1.14.99.39	membrane	bound to	Nitrosomonas europaea	16020	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.99.39	Nitrosomonas europaea	-	-	-

Subunits

EC Number	Subunits	Comment	Organism
1.14.99.39	?	the membrane-bound, active-site-containing 27000 Da polypeptide of ammonia monooxygenase undergoes an aggregation reaction when cells or membranes are heated in the presence of SDS-PAGE. The aggregated protein can be returned to the monomeric state by incubation at high pH in the presence of SDS. Strongly hydrophobic amino acid sequences present in ammonia monooxygenase are responsible for the aggregation phenomenon	Nitrosomonas europaea

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Release 2023.1 (January 2023)