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Fluorometric assay of proteins in the nanogram range

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SPECIFICITY OF AMINO ACID ACYLASES

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Enzymatic deacetylation of histone

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Acetyl-CoA:1,4-diaminobutane N-acetyltransferase occurence in vertebrate organs and subcellular localization

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Acetylation of spermidine and spermine by rat liver and kidney chromatin

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GLUCOSAMINE METABOLISM

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Acetylation and deacetylation of the p-amino group of sulphonamide drugs in animal tissues

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ϵ-Lysine acylase

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Activity of histone deacetylase in rat liver and Novikoff hepatoma

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THE ACETYLATION OF 2-AMINOFLUORENE AND THE DEACETYLATION AND CONCURRENT REACETYLATION OF 2-ACETYLAMINOFLUORENE BY RAT LIVER SLICES

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N-acetyl-β-alanine deacetylase in hog kidney

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Functions of polyamine acetylation

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Histone deacetylase 10 structure and molecular function as a polyamine deacetylase

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Acetylderivatives as intermediates in polyamine catabolism

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Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases

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Polyamines in Mammalian Tumors Part ii

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Polyamines

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Studies of the induction of spermidine/spermine N1-acetyltransferase using a specific antiserum.

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Specific inhibition of polyamine oxidase in vivo is a method for the elucidation of its physiological role

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Polyamines in Mammalian Tumors Part I

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Studies of the specificity and kinetics of rat liver spermidine/spermine N1-acetyltransferase

Ragione, F. D., & Pegg, A. E. (1983) · Biochemical Journal · doi:10.1042/bj2130701 · Cited by 65 · see citing works

Chromatin remodeling by polyamines and polyamine analogs

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Induction of spermidine/spermine N1-acetyltransferase in rat tissues by polyamines

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Polyamine Deacetylase Structure and Catalysis: Prokaryotic Acetylpolyamine Amidohydrolase and Eukaryotic HDAC10

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Structural Basis for the Selective Inhibition of HDAC10, the Cytosolic Polyamine Deacetylase

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Chemical Versatility in Catalysis and Inhibition of the Class IIb Histone Deacetylases

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Binding of N8-Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation

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Formulation of N-acetylputrescine and N1-acetylspermidine in cultured human lymphocytes

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X-ray Crystallographic Snapshots of Substrate Binding in the Active Site of Histone Deacetylase 10

Herbst‐Gervasoni, C. J., & Christianson, D. W. (2021) · Biochemistry · doi:10.1021/acs.biochem.0c00936 · Cited by 22 · see citing works

Effect of carbon tetrachloride on polyamine metabolism in rodent liver

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Biphasic effect of polyamines on chromatin-bound histone deacetylase

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4-Acetamidobutyrate Deacetylase in the Yeast Candida boidinii Grown on Putrescine or Spermidine as Sole Nitrogen Source and Its Probable Role in Polyamine Catabolism

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N1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase

Marchant, P., Manneh, V. A., & Blankenship, J. (1986) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(86)90017-6 · Cited by 13 · see citing works

Structure and Function of the Acetylpolyamine Amidohydrolase from the Deep Earth Halophile Marinobacter subterrani

Osko, J. D., Roose, B. W., Shinsky, S. A., & Christianson, D. W. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00582 · Cited by 13 · see citing works

Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors

Lambona, C., Zwergel, C., Fioravanti, R., Valente, S., & Mai, A. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102668 · Cited by 11 · see citing works

Oxidation of acetylpolyamines by extracellular polyamine oxidase produced by Penicillium sp. No. PO-1

Kobayashi, Y., Higashi, T., Machida, H., Iwasaki, S., & Horikoshi, K. (1983) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(83)90402-8 · Cited by 11 · see citing works

Thermal denaturation of mononucleosomes in the presence of spermine, spermidine, N1-acetylspermidine, N8-acetylspermidine or putrescine: implications for chromosome structure

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Acetylputrescine deacetylase from Micrococcus luteus K-11

Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K., & Matsumoto, T. (1986) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(86)90066-8 · Cited by 6 · see citing works

[57] Acetylspermidine deacetylase (rat liver)

Libby, P. R. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(83)94059-4 · Cited by 6 · see citing works

EFFECT OF ULCERATION ON RAT GASTRIC TISSUE POLYAMINE CONTENTS IN RESPONSE TO DIFFERENT PROCEDURES; INHIBITION OF THESE EFFECTS BY CIMETIDINE

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Polyamine acetylation in the developing and aging mouse brain

Ortíz, J. G., Giacobini, E., & Schmidt‐Glenewinkel, T. (1983) · International Journal of Developmental Neuroscience · doi:10.1016/0736-5748(83)90212-5 · Cited by 2 · see citing works

REFERENCES TO THE ENZYME LIST

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Acetylspermidine deacetylase

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Expression, purification, and crystallization of “humanized” Danio rerio histone deacetylase 10 “HDAC10”, the eukaryotic polyamine deacetylase

Stollmaier, J. G., Herbst‐Gervasoni, C. J., & Christianson, D. W. (2025) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2025.01.074

Inhibition of N⁸-acetylspermidine deacetylation activity of rat liver

Santacroce, M. J. (1980) · Scholarly Commons (University of the Pacific)

N1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase

Marchant, P., Manneh, V. A., & Blankenship, J. (1986) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(86)90017-6 · Cited by 13 · see citing works

Inhibitors for Acetylspermidine Deacetylase from Rat Liver Cytosol

Manneh, V. (1985) · Scholarly Commons (University of the Pacific)

Studies of the specificity and kinetics of rat liver spermidine/spermine N1-acetyltransferase

Ragione, F. D., & Pegg, A. E. (1983) · Biochemical Journal · doi:10.1042/bj2130701 · Cited by 65 · see citing works

Design and synthesis of inhibitors of N8-acetylspermidine deacetylase

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