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Subcellular Compartmentation and Differential Catalytic Properties of the Three Human Nicotinamide Mononucleotide Adenylyltransferase Isoforms

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Berger, Felicitas, Lau, Corinna, Dahlmann, Mathias, Ziegler, Mathias·2005·Journal of Biological Chemistry

DOI 10.1074/jbc.m508660200

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Abstract

Nicotinamide mononucleotide adenylyltransferase (NMNAT) is the central enzyme of the NAD biosynthetic pathway. Three human NMNAT isoforms have recently been identified, but isoform-specific functions are presently unknown, although a tissue-specific role has been suggested. Analyses of the subcellular localization confirmed NMNAT1 to be a nuclear protein, whereas NMNAT2 and -3 were localized to the Golgi complex and the mitochondria, respectively. This differential subcellular localization points to an organelle-specific, nonredundant function of each of the three proteins. Comparison of the kinetic properties showed that particularly NMNAT3 exhibits a high tolerance toward substrate modifications. Moreover, as opposed to preferred NAD+ synthesis by NMNAT1, the other two isoforms could also form NADH directly from the reduced nicotinamide mononucleotide, supporting a hitherto unknown pathway of NAD generation. A variety of physiological intermediates was tested and exerted only minor influence on the catalytic activities of the NMNATs. However, gallotannin was found to be a potent inhibitor, thereby compromising its use as a specific inhibitor of poly-ADP-ribose glycohydrolase. The presence of substrate-specific and independent nuclear, mitochondrial, and Golgi-specific NAD biosynthetic pathways is opposed to the assumption of a general cellular NAD pool. Their existence appears to be consistent with important compartment-specific functions rather than to reflect simple functional redundance.

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Authors: Berger, F., Lau, C., Dahlmann, M., & Ziegler, M.
Affiliations: Freie Universität Berlin (DE)
University of Bergen (NO)
Corresponding author: Ziegler, Mathias
ORCID: Lau, Corinna
Dahlmann, Mathias
Ziegler, Mathias
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2005-10
Volume: 280
Issue: 43
Pages: 36334-36341
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m508660200
OpenAlex: W2068128334
Cited by: 508
References: 52
Citations by year: 2026: 14 · 2025: 30 · 2024: 36 · 2023: 23 · 2022: 29 · 2021: 40 · 2020: 39 · 2019: 35 · 2018: 39 · 2017: 21 · 2016: 22 · 2015: 23 · 2014: 16 · 2013: 23 · 2012: 20
FWCI: 4.24
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5477 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: nicotinamide mononucleotide adenylyltransferase, NAD biosynthesis, subcellular compartmentalization, Golgi apparatus, mitochondria, nuclear localization, enzyme kinetics, substrate tolerance, NADH production, gallotannins, functional redundancy
MeSH terms: Adenosine Triphosphate, Catalysis, Cell Line, Cell Nucleus, Cloning, Molecular, Glycoside Hydrolases, Golgi Apparatus, HeLa Cells, Humans, Kinetics, Nicotinamide-Nucleotide Adenylyltransferase, Poly(ADP-ribose) Polymerases, Protein Conformation, Substrate Specificity, Time Factors, Tissue Distribution, DNA, Complementary, Protein Isoforms, Catalytic Domain, Hydrolyzable Tannins

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Subcellular Compartmentation and Differential Catalytic Properties of the Three Human Nicotinamide Mononucleotide Adenylyltransferase Isoforms

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