AASDHPPT

AASDHPPT
Identifiers
Aliases	AASDHPPT, AASD-PPT, LYS2, LYS5, CGI-80, ACPS, aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
External IDs	OMIM: 607756; MGI: 1914868; GeneCards: AASDHPPT
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2BYD, 2C43, 2CG5
Enzyme activity
Gene location (Human)
Chr.	Chromosome 11 (human)
End	106,098,699 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	4,309,471 bp
RNA expression pattern
	Top expressed in
	sperm; ; Epithelium of choroid plexus; ; frontal pole; ; postcentral gyrus; ; Brodmann area 23; ; superior frontal gyrus; ; superior vestibular nucleus; ; pons; ; cerebellar vermis; ; orbitofrontal cortex;
	Top expressed in
	hand; ; endocardial cushion; ; atrioventricular valve; ; Paneth cell; ; spermatocyte; ; abdominal wall; ; left lobe of liver; ; urothelium; ; transitional epithelium of urinary bladder; ; soleus muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; protein binding; magnesium ion binding; metal ion binding; holo-[acyl-carrier-protein synthase activity];
Cellular component	cytoplasm; cytosol; extracellular exosome;
Biological process	lysine biosynthetic process via aminoadipic acid; pantothenate metabolic process;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	60496
	67618
	ENSG00000149313
	ENSMUSG00000025894
	Q9NRN7
	Q9CQF6
	NM_015423
	NM_026276; NM_001326359
	NP_056238
	NP_001313288; NP_080552
	Wikidata
View/Edit Human	View/Edit Mouse

L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (AASDHPPT) is an enzyme that in humans is encoded by the AASDHPPT gene. It has been suggested that defects in the human gene result in pipecolic acidemia.

The AASDHPPT protein catalyzes the post-translational modification phosphopantetheinylation, in which a 4'-phosphopantetheine (4'-PP) group derived from coenzyme A is covalently attached to target proteins in both cytosol and mitochondria. In the cytosol, these include fatty acid synthase (FASN), aminoadipate semialdehyde dehydrogenase (AASDH), and aldehyde dehydrogenase 1 family member L1 (ALDH1L1), whereas in mitochondria the targets are the mitochondrial acyl carrier protein (mtACP), aldehyde dehydrogenase 1 family member L2 (ALDH1L2), and dehydrogenase/reductase 2 (DHRS2). With the exception of DHRS2, the targets of AASDHPPT contain a acyl carrier protein (ACP) domain, a cofactor domain widespread across bacteria and eukaryotes with roles in the synthesis of fatty acids, polyketides, and nonribosomal peptides.

The protein encoded by this gene is similar to Saccharomyces cerevisiae LYS5, which is required for the activation of the alpha-aminoadipate dehydrogenase in the biosynthetic pathway of lysine. Yeast alpha-aminoadipate dehydrogenase converts alpha-biosynthetic-aminoadipate semialdehyde to alpha-aminoadipate.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000149313 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025894 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Joshi AK, Zhang L, Rangan VS, Smith S (August 2003). "Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity". The Journal of Biological Chemistry. 278 (35): 33142–33149. doi:10.1074/jbc.M305459200. PMID 12815048.
↑ Praphanphoj V, Sacksteder KA, Gould SJ, Thomas GH, Geraghty MT (April 2001). "Identification of the alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene". Molecular Genetics and Metabolism. 72 (4): 336–342. doi:10.1006/mgme.2000.3138. PMID 11286508.
1 2 "Entrez Gene: AASDHPPT aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase".
1 2 Norden PR, Wedan RJ, Preston SE, Canfield M, Graber N, Longenecker JZ, et al. (2024-05-10). "Mitochondrial Phosphopantetheinylation is Required for Oxidative Function". bioRxiv 10.1101/2024.05.09.592977.
↑ "InterPro". InterPro.