1.7.2.4: nitrous-oxide reductase

This is an abbreviated version!
For detailed information about nitrous-oxide reductase, go to the full flat file.

Word Map on EC 1.7.2.4

1.7.2.4

denitrification

denitrify

nitrite

greenhouse

denitrificans

paracoccus

stutzeri

dinitrogen

wastewater

binuclear

tetranuclear

cycloclastes

mixed-valence

multicopper

ammonia-oxidizing

n-cycle

nautica

wolinella

arable

nitrospirae

stratospheric

agriculture

t-rflp

degradation

Reaction

nitrogen

+

H2O

+

2 ferricytochrome c

=

nitrous oxide

+ 2 ferrocytochrome c + 2 H+

Synonyms

cNosZ, EC 1.7.99.6, HdN2OR, McoP, MhN2OR, multicopper oxidase, N(2)OR, N2O reductase, N2OR, nitrous oxide reductase, NosZ, PpN2OR, PsN2OR, Sden_2219, SdN2OR, Z-type N2OR

ECTree

1 Oxidoreductases

1.7 Acting on other nitrogenous compounds as donors

1.7.2 With a cytochrome as acceptor

1.7.2.4 nitrous-oxide reductase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
1	Activating Compound
4524	AA Sequence
4	Application
1	CAS Registry Number
15	Cloned(Commentary)
10	Cofactor
7	Crystallization (Commentary)
5	Expression
20	General Information
3	General Stability
33	Inhibitors
2	kcat/KM [mM/s]
7	Ki Value [mM]
16	KM Value [mM]
12	Localization
64	Metals/Ions
40	Molecular Weight [Da]
77	Natural Substrates/ Products (Substrates)
154	Organism
1	Oxidation Stability
8	Pathway
48	PDB ID
8	pH Optimum
5	pH Range
1	Posttranslational Modification
21	Protein Variants
20	Purification (Commentary)
3	Reaction
3	Reaction Type
116	Reference
3	Source Tissue
38	Specific Activity [micromol/min/mg]
3	Storage Stability
148	Substrates and Products (Substrate)
41	Subunits
154	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
3	Temperature Stability [°C]
3	Turnover Number [1/s]

Engineering

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Engineering on EC 1.7.2.4 - nitrous-oxide reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

back to the top

Go to Protein Variants Search

C165G

show

C622D

Pseudomonas stutzeri

-

no activity, distorted CuA-centre

E296Q

Pyrobaculum aerophilum

-

mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type

M297A

Pyrobaculum aerophilum

-

mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type

M389A

Pyrobaculum aerophilum

-

mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type

W355A

Pyrobaculum aerophilum

-

mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type

D576A

Stutzerimonas stutzeri

the mutant shows specific activity comparable to the wild type enzyme

D576A/S550A

Stutzerimonas stutzeri

the mutant shows decreased specific activity compared to the wild type enzyme

H583A

Stutzerimonas stutzeri

inactive

H583D

Stutzerimonas stutzeri

the oxidation rate of the CuA site in the mutant enzyme is much lower than that of wild type

H583E

Stutzerimonas stutzeri

the oxidation rate of the CuA site in the mutant enzyme is much lower than that of wild type

H583F

Stutzerimonas stutzeri

inactive

H583K

Stutzerimonas stutzeri

inactive

H583N

Stutzerimonas stutzeri

inactive

H583W

Stutzerimonas stutzeri

inactive

H583Y

Stutzerimonas stutzeri

the mutant has a redox-inert CuA site

H583Y/D576A

Stutzerimonas stutzeri

inactive although CuZ is still present

additional information

show

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)