Nicotinate dehydrogenase (cytochrome): Difference between revisions

Search
PMC	articles
PubMed	articles
NCBI	proteins

Nicotinate dehydrogenase (cytochrome)
Nicotinate dehydrogenase (cytochrome)
Identifiers
EC no.	1.17.2.1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Browse history interactively

← Previous edit

Content deleted Content added

VisualWikitext

Inline

Latest revision as of 15:09, 26 August 2023

Nicotinate dehydrogenase (cytochrome) (EC 1.17.2.1, nicotinic acid hydroxylase, nicotinate hydroxylase) is an enzyme with systematic name nicotinate:cytochrome 6-oxidoreductase (hydroxylating).^[1]^[2] This enzyme catalyses the following chemical reaction

nicotinate + a ferricytochrome + H₂O

\rightleftharpoons

6-hydroxynicotinate + a ferrocytochrome + 2 H⁺

This two-component enzyme from Pseudomonas belongs to the family of xanthine dehydrogenases.

References

^ Jiménez JI, Canales A, Jiménez-Barbero J, Ginalski K, Rychlewski L, García JL, Díaz E (August 2008). "Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440". Proceedings of the National Academy of Sciences of the United States of America. 105 (32): 11329–34. doi:10.1073/pnas.0802273105. PMC 2516282. PMID 18678916.
^ Yang Y, Yuan S, Chen T, Ma P, Shang G, Dai Y (July 2009). "Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440". Biodegradation. 20 (4): 541–9. doi:10.1007/s10532-008-9243-x. PMID 19118407. S2CID 23219659.

External links

Nicotinate+dehydrogenase+(cytochrome) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Jiménez JI, Canales A, Jiménez-Barbero J, Ginalski K, Rychlewski L, García JL, Díaz E (August 2008). "Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440". Proceedings of the National Academy of Sciences of the United States of America. 105 (32): 11329–34. doi:10.1073/pnas.0802273105. PMC 2516282. PMID 18678916.

[2] Yang Y, Yuan S, Chen T, Ma P, Shang G, Dai Y (July 2009). "Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440". Biodegradation. 20 (4): 541–9. doi:10.1007/s10532-008-9243-x. PMID 19118407. S2CID 23219659.

[1]

[2]

@@ Line 1: / Line 1: @@
 {{Infobox enzyme
-| Name = Nicotinate dehydrogenase (cytochrome)
+| Name       = Nicotinate dehydrogenase (cytochrome)
-| EC_number = 1.17.2.1
+| EC_number  = 1.17.2.1
 | CAS_number =
+| GO_code    =
-| IUBMB_EC_number = 1/17/2/1
-| GO_code =
+| image      =
-| image =
+| width      =
-| width =
+| caption    =
-| caption =
 }}
-'''Nicotinate dehydrogenase ([[cytochrome]])''' ({{EC number|1.17.2.1}}, ''nicotinic acid hydroxylase'', ''nicotinate hydroxylase'') is an [[enzyme]] with system name ''nicotinate:cytochrome 6-oxidoreductase (hydroxylating)''.<ref>{{cite journal | title = Deciphering the genetic determinants for aerobic nicotinic acid degradation: the <em>nic</em> cluster from <em>Pseudomonas putida</em> KT2440 |author = Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. |journal = Proc. Natl. Acad. Sci. USA |year = 2008 |volume = 105 |pages = 11329–11334 |pmid = 18678916 |doi=10.1073/pnas.0802273105 |pmc=2516282}}</ref><ref>{{cite journal | title = Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from <em>Pseudomonas putida</em> KT2440 |author = Yang, Y., Yuan, S., Chen, T., Ma, P., Shang, G. and Dai, Y. |journal = Biodegradation |year = 2009 |volume = 20 |pages = 541–549 |pmid = 19118407 |doi=10.1007/s10532-008-9243-x |issue=4}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
+'''Nicotinate dehydrogenase ([[cytochrome]])''' ({{EC number|1.17.2.1}}, ''nicotinic acid hydroxylase'', ''nicotinate hydroxylase'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''nicotinate:cytochrome 6-oxidoreductase (hydroxylating)''.<ref>{{cite journal | vauthors = Jiménez JI, Canales A, Jiménez-Barbero J, Ginalski K, Rychlewski L, García JL, Díaz E | title = Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 32 | pages = 11329–34 | date = August 2008 | pmid = 18678916 | pmc = 2516282 | doi = 10.1073/pnas.0802273105 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Yang Y, Yuan S, Chen T, Ma P, Shang G, Dai Y | title = Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440 | journal = Biodegradation | volume = 20 | issue = 4 | pages = 541–9 | date = July 2009 | pmid = 19118407 | doi = 10.1007/s10532-008-9243-x | s2cid = 23219659 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
+[[File:Nicotinate dehydrogenase (cytochrome).svg|center|400px]]
-: [[nicotinate]] + a [[ferricytochrome]] + H<sub>2</sub>O <math>\rightleftharpoons</math> 6-hydroxynicotinate + a ferrocytochrome + 2 H<sup>+</sup>
+<div align=center><small>[[nicotinate]] + a [[ferricytochrome]] + H<sub>2</sub>O <math>\rightleftharpoons</math> 6-hydroxynicotinate + a ferrocytochrome + 2 H<sup>+</sup></small></div>
 This two-component enzyme from ''[[Pseudomonas]]'' belongs to the family of [[xanthine]] dehydrogenases.
-== References ==
-{{reflist}}
 == See also ==
 * [[Nicotinate dehydrogenase]]
+== References ==
+{{reflist}}
 == External links ==
 * {{MeshName|Nicotinate+dehydrogenase+(cytochrome)}}
+{{Other oxidoreductases}}
+{{Enzymes}}
+{{Portal bar|Biology|border=no}}
 [[Category:EC 1.17.2]]

v t e Other oxidoreductases (EC 1.15–1.21)
1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3
1.16: Oxidizing metal ions	Ceruloplasmin (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase 7-Hydroxymethyl chlorophyll a reductase
1.18: Acting on iron–sulfur proteins as donors	Nitrogenase
1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)
1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5
1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)