nicotinamidase

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nicotinamidase
Identifiers
EC number	3.5.1.19
CAS number	9033-32-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
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PMC	articles
PubMed	articles
NCBI	proteins

ニコチンアミダーゼ

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/03/29 15:54:36」(JST)

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In enzymology, a nicotinamidase (EC 3.5.1.19) is an enzyme that catalyzes the chemical reaction

nicotinamide + H₂O

\rightleftharpoons

nicotinate + NH₃

Thus, the two substrates of this enzyme are nicotinamide and H₂O, whereas its two products are nicotinate and NH₃.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is nicotinamide amidohydrolase. Other names in common use include nicotinamide deaminase, nicotinamide amidase, and YNDase. This enzyme participates in nicotinate and nicotinamide metabolism.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1ILW, 1IM5, and 2H0R.

References

Petrack B, Greengard P, Craston A, Sheppy F (1965). "Nicotinamide deamidase from mammalian liver". J. Biol. Chem. 240: 1725–1730. PMID 14285515.
Sarma DS, Rajalakshmi S, Sarma S (1964). "Studies on the enzymes involved in nicotinamide adenine dinucleotide metabolism in Aspergillus niger". Biochim. Biophys. Acta. 81: 311–322. doi:10.1016/0926-6569(64)90047-1.

This EC 3.5 enzyme-related article is a stub. You can help Wikipedia by expanding it.

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1. 結核の自然史、微生物学、および病因 natural history microbiology and pathogenesis of tuberculosis

English Journal

Pnc1 piggy-back import into peroxisomes relies on Gpd1 homodimerisation.

Saryi NA1, Hutchinson JD1, Al-Hejjaj MY1, Sedelnikova S1, Baker P1, Hettema EH1.
Scientific reports.Sci Rep.2017 Feb 17;7:42579. doi: 10.1038/srep42579.
PMID 28209961

Key role of an ADP - ribose - dependent transcriptional regulator of NAD metabolism for fitness and virulence of Pseudomonas aeruginosa.

Okon E1, Dethlefsen S1, Pelnikevich A1, Barneveld AV1, Munder A2, Tümmler B3.
International journal of medical microbiology : IJMM.Int J Med Microbiol.2017 Jan;307(1):83-94. doi: 10.1016/j.ijmm.2016.09.007. Epub 2016 Nov 5.
PMID 27865623

Detecting Mutations in the Mycobacterium tuberculosis Pyrazinamidase Gene pncA to Improve Infection Control and Decrease Drug Resistance Rates in Human Immunodeficiency Virus Coinfection.

Dudley MZ1, Sheen P2,3, Gilman RH1,3,4, Ticona E5,6, Friedland JS7, Kirwan DE8,9, Caviedes L3, Rodriguez R10, Cabrera LZ4, Coronel J3, Grandjean L3,7, Moore DA3,4,11, Evans CA7,12, Huaroto L5,13, Chávez-Pérez V5,13, Zimic M14,3.
The American journal of tropical medicine and hygiene.Am J Trop Med Hyg.2016 Dec 7;95(6):1239-1246. Epub 2016 Oct 24.
PMID 27928075

Japanese Journal

寿命とニコチンアミド(高齢者とB群ビタミン)

柴田克己
ビタミン 79(11), 531-538, 2005-11-25
… In 2003, as for the extension of the longevity that induced by the energy restriction, it was reported that it happened through increasing the appearance of PNC1 (a gene that codes nicotinamidase), and however, the effect disappeared due to the lack of Sir2. … From these reports, I have thought that it becomes a key that extends longevity that the relation between the Sir2 protein (NAD^+-dependence histone deacetylase) and nicotinamidase controls aging. …
NAID 110004857272

1. ユーグレナにおけるNADの生合成と代謝の経路に関する検討

西谷弘,黒宮友美,緒方進 [他],奥村克純,田口寛
ビタミン 75(1), 15-21, 2001-01-25
… Among enzymes related to NAD biosynthesis and metabolism, nicotinamidase, nicotinate phosphoribosyltransferase, nicotinic acid mononucleotide adenyltransferase, and NAD synthetase activities were all found in Euglena gracilis Z. … Nicotinate phosphoribosyltransferase was inhibited by nicotinic acid mononucleotide and nicotinic acid adenine dinucleotide, whereas nicotinamidase by nicotinamide mononucleotide, NAD, and N^1-methylnicotinamide. …
NAID 110002883430

Mutations in pncA, a gene encoding pyrazinamidase/nicotinamidase, cause resistance to the antituberculous drug pyrazinamide in tubercle bacillus

SCORPIO A.
Nat Med 2, 662-667, 1996
NAID 80008988860

Related Pictures

Streptococcus pneumoniae Nicotinamidase Nicotinamidase modulation of NAD 157591.fig.002 biosynthesis of NAD(P)+. Nicotinamidase nicotinamidase (pcn-1) Nicotinamidase ; Nicotinamide

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

v t e Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

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)

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