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Literature summary for 3.5.1.62 extracted from

  • Shinsky, S.A.; Christianson, D.W.
    Polyamine deacetylase structure and catalysis prokaryotic acetylpolyamine amidohydrolase and eukaryotic HDAC10 (2018), Biochemistry, 57, 3105-3114 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.62

Inhibitors

Inhibitors Comment Organism Structure
7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one AAT, binds as a tetrahedral gem-diolate to both APAH and HDAC10 (histone 10 deacetylase, EC 3.5.1.48), thereby mimicking the tetrahedral intermediate and its flanking transition states in catalysis Mycoplana ramosa

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ catalytic zinc ion Mycoplana ramosa

Organism

Organism UniProt Comment Textmining
Mycoplana ramosa Q48935
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information acetylpolyamine amidohydrolase (APAH) from Mycoplana ramosa, is a broad-specificity polyamine deacetylase Mycoplana ramosa ?
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 ?

Subunits

Subunits Comment Organism
dimer alpha/beta fold. The quaternary structure, i.e. dimer assembly, provides the steric constriction that directs the polyamine substrate specificity of APAH Mycoplana ramosa

Synonyms

Synonyms Comment Organism
acetylpolyamine amidohydrolase
-
 Mycoplana ramosa
APAH
-
 Mycoplana ramosa

General Information

General Information Comment Organism
evolution the enzyme adopts the characteristic arginase-deacetylase fold and employ a Zn2+-activated water molecule for catalysis. The active sites of HDAC10 (histone 10 deacetylase, EC 3.5.1.48) and APAH are sterically constricted to enforce specificity for long, slender polyamine substrates and exclude bulky peptides and proteins containing acetyl-L-lysine. The quaternary structure, i.e., dimer assembly, provides the steric constriction that directs the polyamine substrate specificity of APAH. Structure and catalytic mechanism of polyamine deacetylases, comparison of HDAC and APAH, overview Mycoplana ramosa
additional information nucleophilic attack of Zn2+-bound water at the amide carbonyl group polarized by Zn2+ and the catalytic tyrosine is facilitated by a general base. The Zn2+ ion, tyrosine, and tandem histidine residues contribute to transition state stabilization in each deacetylase. Collapse of the tetrahedral intermediate requires a proton donor, and the second histidine of the tandem pair must serve as the general acid due to its proximity to the leaving amino group. Structure-function analysis of substrate specificity, overview Mycoplana ramosa