Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse

Alexander K.H. Weiss; Andreas Naschberger; Elia Cappuccio; Christina Metzger; Lorenza Mottes; Max Holzknecht; Jill Von Velsen; Matthew W. Bowler; Bernhard Rupp; Pidder Jansen-Dürr

doi:10.1042/BSR20194431

Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse

Alexander K.H. Weiss, Andreas Naschberger, Elia Cappuccio, Christina Metzger, Lorenza Mottes, Max Holzknecht, Jill Von Velsen, Matthew W. Bowler, Bernhard Rupp, Pidder Jansen-Dürr

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.

Original language	English (US)
Journal	Bioscience reports
Volume	40
Issue number	3
DOIs	https://doi.org/10.1042/BSR20194431
State	Published - Jan 1 2020
Externally published	Yes

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Generated from Scopus record by KAUST IRTS on 2023-02-15

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title = "Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse",

abstract = "FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.",

author = "Weiss, {Alexander K.H.} and Andreas Naschberger and Elia Cappuccio and Christina Metzger and Lorenza Mottes and Max Holzknecht and {Von Velsen}, Jill and Bowler, {Matthew W.} and Bernhard Rupp and Pidder Jansen-D{\"u}rr",

note = "Generated from Scopus record by KAUST IRTS on 2023-02-15",

year = "2020",

month = jan,

day = "1",

doi = "10.1042/BSR20194431",

language = "English (US)",

volume = "40",

journal = "Bioscience reports",

issn = "0144-8463",

publisher = "Portland Press Ltd.",

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TY - JOUR

T1 - Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse

AU - Weiss, Alexander K.H.

AU - Naschberger, Andreas

AU - Cappuccio, Elia

AU - Metzger, Christina

AU - Mottes, Lorenza

AU - Holzknecht, Max

AU - Von Velsen, Jill

AU - Bowler, Matthew W.

AU - Rupp, Bernhard

AU - Jansen-Dürr, Pidder

N1 - Generated from Scopus record by KAUST IRTS on 2023-02-15

PY - 2020/1/1

Y1 - 2020/1/1

N2 - FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.

AB - FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.

UR - https://portlandpress.com/bioscirep/article/40/3/BSR20194431/222164/Structural-and-functional-comparison-of

UR - http://www.scopus.com/inward/record.url?scp=85081150294&partnerID=8YFLogxK

U2 - 10.1042/BSR20194431

DO - 10.1042/BSR20194431

M3 - Article

SN - 0144-8463

VL - 40

JO - Bioscience reports

JF - Bioscience reports

IS - 3

ER -

Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse

Abstract

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