EzCatDB: S00031
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DB codeS00031
CATH domainDomain 11.10.630.10 : Cytochrome p450Catalytic domain
E.C.1.7.1.14

CATH domainRelated DB codes (homologues)
1.10.630.10 : Cytochrome p450S00033,M00154,S00030

Enzyme Name
UniProtKBKEGG

P23295
Protein nameCytochrome P450 55A1nitric oxide reductase [NAD(P), nitrous oxide-forming]
fungal nitric oxide reductase
cytochrome P450nor
NOR (ambiguous)
SynonymsEC 1.14.-.-
CYPLVA1
P450 DNIR
Nitric oxide reductase
P450nor
PfamPF00067 (p450)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00910Nitrogen metabolism

UniProtKB:Accession NumberP23295
Entry nameNOR_FUSOX
ActivityNitrous oxide + NAD(P)(+) + H(2)O = 2 nitric oxide + NAD(P)H.
Subunit
Subcellular location
CofactorHeme group.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00032C00533C00004C00005C00080C00887C00003C00006C00001
CompoundHemeNitric oxideNADHNADPHH+Nitrous oxideNADNADP+H2O
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metalothersamide group,amine group,nucleotideamide group,amine group,nucleotideothersothersamide group,amine group,nucleotideamide group,amine group,nucleotideH2O
ChEBI17627
26355
16480
16908
16474
15378
17045
15846
18009
15377

PubChem
145068
439153
5884
1038
948
5893
5886
962
22247451

                  
1cl6ABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Intermediate-bound:HEM-_NO
1cmjABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Intermediate-bound:HEM-_NO
1cmnABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Intermediate-bound:HEM-_NO
1eheABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Unbound
1ehfABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Unbound
1ehgABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Unbound
1f24ABound:HEMBound:_NOUnboundUnbound UnboundUnboundUnbound Unbound
1f25ABound:HEMBound:_NOUnboundUnbound UnboundUnboundUnbound Unbound
1f26ABound:HEMBound:_NOUnboundUnbound UnboundUnboundUnbound Unbound
1gedABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Unbound
1geiABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Intermediate-analogue:HEM-NBN
1gejABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Intermediate-analogue:HEM-NBN
1jfbABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Unbound
1jfcABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Intermediate-analogue:HEM-CMO
1romABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Unbound
2romABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Intermediate-analogue:HEM-CMO
1ulwABound:HEMUnboundUnboundUnbound UnboundUnboundUnbound Unbound
1xqdABound:HEMUnboundUnboundUnbound UnboundAnalogue:DNDUnbound Unbound

Active-site residues
resource
literature [8], [9], [13], [14], [15]
pdbCatalytic residuesCofactor-binding residuescomment
           
1cl6ATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1cmjATHR 243;       ;ASP 393
CYS 352(Heme iron binding)
mutant S286T
1cmnATHR 243;       ;ASP 393
CYS 352(Heme iron binding)
mutant S286V
1eheATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1ehfATHR 243;       ;ASP 393
CYS 352(Heme iron binding)
mutant S286T
1ehgATHR 243;       ;ASP 393
CYS 352(Heme iron binding)
mutant S286V
1f24A       ;SER 286;ASP 393
CYS 352(Heme iron binding)
mutant T243A
1f25A       ;SER 286;ASP 393
CYS 352(Heme iron binding)
mutant T243N
1f26A       ;SER 286;ASP 393
CYS 352(Heme iron binding)
mutant T243V
1gedATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1geiATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1gejATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1jfbATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1jfcATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1romATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
2romATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1ulwATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 
1xqdATHR 243;SER 286;ASP 393
CYS 352(Heme iron binding)
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.1622-1623
[5]

[7]

[9]p.830-831
[10]p.8845-8846
[11]Fig.2, p.12965
[14]p.4824-4825
[15]p.107
[16]

[22]Fig.2
[24]p.212-214

references
[1]
PubMed ID8196045
JournalJ Mol Biol
Year1994
Volume239
Pages158-9
AuthorsNakahara K, Shoun H, Adachi S, Iizuka T, Shiro Y
TitleCrystallization and preliminary X-ray diffraction studies of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum.
[2]
PubMed ID7619804
JournalBiochemistry
Year1995
Volume34
Pages9052-8
AuthorsShiro Y, Fujii M, Isogai Y, Adachi S, Iizuka T, Obayashi E, Makino R, Nakahara K, Shoun H
TitleIron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum: relevance to its NO reduction activity.
[3]
PubMed ID7829493
JournalJ Biol Chem
Year1995
Volume270
Pages1617-23
AuthorsShiro Y, Fujii M, Iizuka T, Adachi S, Tsukamoto K, Nakahara K, Shoun H
TitleSpectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism.
[4]
PubMed ID9010609
JournalBiochimie
Year1996
Volume78
Pages792-9
AuthorsKudo T, Tomura D, Liu DL, Dai XQ, Shoun H
TitleTwo isozymes of P450nor of Cylindrocarpon tonkinense: molecular cloning of the cDNAs and genes, expressions in the yeast, and the putative NAD(P)H-binding site.
[5]
JournalJ Biol Inorg Chem
Year1996
Volume1
Pages372-6
AuthorsRietjens IM, Osman AM, Veeger C, Zakharieva O, Antony J, Grodzicki M, Trautwein AX
TitleOn the role of the axial ligand in heme-based catalysis of the peroxidase and P450 type.
[6]
PubMed ID9003438
JournalBiochim Biophys Acta
Year1997
Volume1337
Pages66-74
AuthorsImai Y, Okamoto N, Nakahara K, Shoun H
TitleAbsorption spectral studies on heme ligand interactions of P-450nor.
[7]
PubMed ID9074619
JournalBiochim Biophys Acta
Year1997
Volume1338
Pages93-9
AuthorsToritsuka N, Shoun H, Singh UP, Park SY, Iizuka T, Shiro Y
TitleFunctional and structural comparison of nitric oxide reductases from denitrifying fungi Cylindrocarpon tonkinense and Fusarium oxysporum.
[8]
PubMed ID9256249
JournalFEBS Lett
Year1997
Volume412
Pages346-50
AuthorsPark SY, Shimizu H, Adachi S, Shiro Y, Iizuka T, Nakagawa A, Tanaka I, Shoun H, Hori H
TitleCrystallization, preliminary diffraction and electron paramagnetic resonance studies of a single crystal of cytochrome P450nor.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID97475224
PubMed ID9334748
JournalNat Struct Biol
Year1997
Volume4
Pages827-32
AuthorsPark SY, Shimizu H, Adachi S, Nakagawa A, Tanaka I, Nakahara K, Shoun H, Obayashi E, Nakamura H, Iizuka T, Shiro Y
TitleCrystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum.
Related PDB1rom,2rom
Related UniProtKBP23295
[10]
PubMed ID9636024
JournalBiochemistry
Year1998
Volume37
Pages8839-47
AuthorsOkamoto N, Imai Y, Shoun H, Shiro Y
TitleSite-directed mutagenesis of the conserved threonine (Thr243) of the distal helix of fungal cytochrome P450nor.
[11]
JournalJ Am Chem Soc
Year1998
Volume120
Pages12964-65
AuthorsObayashi E, Takahashi S, Shiro Y
TitleElectronic structure of reaction intermediate of cytochrome P450nor in its nitric oxide reduction.
[12]
PubMed ID10369184
JournalNitric Oxide
Year1999
Volume3
Pages142-52
AuthorsMehl M, Daiber A, Herold S, Shoun H, Ullrich V
TitlePeroxynitrite reaction with heme proteins.
[13]
PubMed ID11004439
JournalBiochim Biophys Acta
Year2000
Volume1459
Pages266-73
AuthorsHendriks J, Oubrie A, Castresana J, Urbani A, Gemeinhardt S, Saraste M
TitleNitric oxide reductases in bacteria.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID20138220
PubMed ID10671516
JournalJ Biol Chem
Year2000
Volume275
Pages4816-26
AuthorsShimizu H, Obayashi E, Gomi Y, Arakawa H, Park SY, Nakamura H, Adachi S, Shoun H, Shiro Y
TitleProton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes.
Related PDB1cl6,1cmj,1cmn
Related UniProtKBP23295
[15]
CommentsX-ray crystallography
PubMed ID11132616
JournalJ Inorg Biochem
Year2000
Volume82
Pages103-11
AuthorsObayashi E, Shimizu H, Park SY, Shoun H, Shiro Y
TitleMutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function.
Related PDB1f24,1f25,1f26
[16]
CommentsX-ray crystallography
PubMed ID11051564
JournalJ Inorg Biochem
Year2000
Volume81
Pages191-205
AuthorsShimizu H, Park S, Lee D, Shoun H, Shiro Y
TitleCrystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s.
Related PDB1ehe,1ehf,1ehg
[17]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)
Medline ID21159060
PubMed ID11258878
JournalBiochemistry
Year2001
Volume40
Pages2669-77
AuthorsLee DS, Park SY, Yamane K, Obayashi E, Hori H, Shiro Y
TitleStructural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.
Related PDB1gei,1gej
Related UniProtKBP23295
[18]
CommentsX-ray crystallography
PubMed ID11076941
JournalJ Biol Chem
Year2001
Volume276
Pages5020-6
AuthorsKudo T, Takaya N, Park SY, Shiro Y, Shoun H
TitleA positively charged cluster formed in the heme-distal pocket of cytochrome P450nor is essential for interaction with NADH.
Related PDB1ged
[19]
PubMed ID11346959
JournalPlanta
Year2001
Volume212
Pages835-41
AuthorsStohr C, Strube F, Marx G, Ullrich WR, Rockel P
TitleA plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite.
[20]
CommentsX-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS)
Medline ID21620774
PubMed ID11752781
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages81-9
AuthorsShimizu H, Park SY, Shiro Y, Adachi S
TitleX-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution.
Related PDB1jfb,1jfc
Related UniProtKBP23295
[21]
PubMed ID12105197
JournalJ Biol Chem
Year2002
Volume277
Pages33842-7
AuthorsZhang L, Kudo T, Takaya N, Shoun H
TitleThe B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH.
[22]
JournalJ Mol Struct Theochem
Year2003
Volume624
Pages309-22
AuthorsTsukamoto K, Nakamura S, Shimizu K
TitleSAM1 semiempirical calculations on the catalytic cycle of nitric oxide reductase from Fusarium oxysporum.
[23]
PubMed ID14766741
JournalJ Biol Chem
Year2004
Volume279
Pages17120-5
AuthorsGronberg KL, Watmough NJ, Thomson AJ, Richardson DJ, Field SJ
TitleRedox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.
[24]
PubMed ID15313618
JournalJ Mol Biol
Year2004
Volume342
Pages207-17
AuthorsOshima R, Fushinobu S, Su F, Zhang L, Takaya N, Shoun H
TitleStructural evidence for direct hydride transfer from NADH to cytochrome P450nor.
Related PDB1ulw,1xqd

comments
Although Swissprot data, P23295, reports that E.C. number of this enzyme is 1.14.-.-, it has been transferred to 1.7.1.14.
NAD is used as an "acceptor", whilst NADH is used as a "reduced acceptor" in this enzyme.
This enzyme catalyzes three successive reactions as follows (see [18]; These reactions are irreversible.):
(A) Fe3+ + NO -> Fe3+-NO
(B) Fe3+-NO + NADH -> Intermediate + NAD+
(C) Intermediate + NO + H+ -> Fe3+ + N2O +H2O

createdupdated
2004-05-172012-10-03


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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