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maize-b6t1C9

Zea mays (Maize) ZmB6T1C9 ZmAPT2 Zm.98376 Acyl-protein thioesterase 2

Comment

Burger et al.<\/A> show that Acyl-protein thioesterase structures present a long tunnel for accommodation of long-chain fatty acids and release the product by use of a flexible loop tunnel lid. Homologous deacetylases use a hydrophobic residue to fix the lid and another residue to close the tunnel entrance. This causes loop rigidity changing the catalytic preference to deacetylation. ZmB6T1C9 as its paralogue in Arabidopsis At5G20060 is an acylprotein thioesterase and not an protein deacetylase

Relationship

Family : LYsophospholipase_carboxylesterase

Block : X

Position in NCBI Life Tree : Zea mays

Molecular evidence

No mutation

No kinetic

No disease

No substrate

No inhibitor

Database

Sequence

Peptide

MSYGGSSSLA PGAKRPFEYG RTHVVRPKGT HKATIVWLHG LGDNGTSWSQ LLETLPLPNI KWICPTAPSR PVSLFGGFPC TAWFDVADLS EDAPDDTEGM DASAAHVANL LSTEPADIKL GVGGFSMGAA TALYSATCFA HGKYGNGNPY PVNLSLAVGL SGWLPCARTL KNRIEASPEA AQRASTIPLL LCHGKADDVV LYKHGQRSTD ALKANGFSNV LFKSYNSLGH YTVPEEMDEV CKWLTANLGL GTSSS

References

Title : A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors - Burger_2017_Nat.Commun_8_2201
Author(s) : Burger M , Willige BC , Chory J
Ref : Nat Commun , 8 :2201 , 2017
Abstract : Burger_2017_Nat.Commun_8_2201
ESTHER : Burger_2017_Nat.Commun_8_2201
PubMedSearch : Burger_2017_Nat.Commun_8_2201
PubMedID: 29259199
Gene_locus related to this paper: maize-b6t1C9 , arath-SOBR1 , arath-SOBRL , arath-AT5G20060