Literature summary for 1.9.6.1 extracted from

Thomas, G.; Potter, L.; Cole, J.A.
The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site (1999), FEMS Microbiol. Lett., 174, 167-171.

Search for more literature for 1.9.6.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli K-12

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Escherichia coli K-12	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mo	molybdoprotein	Escherichia coli K-12

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
16000	-	1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE	Escherichia coli K-12
90000	-	1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE	Escherichia coli K-12

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli K-12	P33937 and P0ABL3	P33937: napA, P0ABL3: napB	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the pre-NapA leader sequence is both unexpectedly long and, unless two successive proteolysis steps are involved, is cleaved at the unprecedented sequence G-Q-Q	Escherichia coli K-12

Storage Stability

Storage Stability	Organism
4°C, about 90% of the activity is lost after 48 h, no activity remains after 4 days	Escherichia coli K-12

Subunits

Subunits	Comment	Organism
heterodimer	1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE	Escherichia coli K-12

Synonyms

Synonyms	Comment	Organism
NapA	-	Escherichia coli K-12

Cofactor

Cofactor	Comment	Organism	Structure
heme	subunit NapB is a diheme cytochrome c	Escherichia coli K-12

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Release 2023.1 (January 2023)