ALDH4A1

From Wikipedia, the free encyclopedia

Aldehyde dehydrogenase 4 family, member A1

Identifiers

ALDH4A1; ALDH4; P5CD; P5CDh; P5CDhL; P5CDhS

External IDs

OMIM: 606811 MGI: 2443883 HomoloGene: 6081

Gene ontology
Molecular Function:	• 1-pyrroline-5-carboxylate dehydrogenase activity • aldehyde dehydrogenase (NAD) activity • electron carrier activity • oxidoreductase activity
Cellular Component:	• mitochondrion • mitochondrial matrix
Biological Process:	• proline biosynthetic process • proline catabolic process • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003748 (mRNA)
NP_003739 (protein)

NM_175438 (mRNA)
NP_780647 (protein)

Location

Chr 1: 19.07 - 19.1 Mb

Chr 4: 138.89 - 138.92 Mb

Pubmed search

[1]

[2]

Aldehyde dehydrogenase 4 family, member A1, also known as ALDH4A1, is a human gene.^[1]

This protein belongs to the aldehyde dehydrogenase family of proteins. This enzyme is a mitochondrial matrix NAD-dependent dehydrogenase which catalyzes the second step of the proline degradation pathway, converting pyrroline-5-carboxylate to glutamate. Deficiency of this enzyme is associated with type II hyperprolinemia, an autosomal recessive disorder characterized by accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. Two transcript variants encoding the same protein have been identified for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: ALDH4A1 aldehyde dehydrogenase 4 family, member A1.

[edit] Further reading

Valle D, Goodman SI, Harris SC, Phang JM (1980). "Genetic evidence for a common enzyme catalyzing the second step in the degradation of proline and hydroxyproline.". J. Clin. Invest. 64 (5): 1365–70. PMID 500817.
Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison.". Electrophoresis 13 (12): 992–1001. PMID 1286669.
Goodman SI, Mace JW, Miles BS, et al. (1974). "Defective hydroxyproline metabolism in type II hyperprolinemia.". Biochemical medicine 10 (4): 329–36. PMID 4851275.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Hu CA, Lin WW, Valle D (1996). "Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase.". J. Biol. Chem. 271 (16): 9795–800. PMID 8621661.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Geraghty MT, Vaughn D, Nicholson AJ, et al. (1998). "Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia.". Hum. Mol. Genet. 7 (9): 1411–5. PMID 9700195.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Twizere JC, Kruys V, Lefèbvre L, et al. (2004). "Interaction of retroviral Tax oncoproteins with tristetraprolin and regulation of tumor necrosis factor-alpha expression.". J. Natl. Cancer Inst. 95 (24): 1846–59. PMID 14679154.
Yoon KA, Nakamura Y, Arakawa H (2004). "Identification of ALDH4 as a p53-inducible gene and its protective role in cellular stresses.". J. Hum. Genet. 49 (3): 134–40. doi:10.1007/s10038-003-0122-3. PMID 14986171.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.

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v • d • e Aldehyde/oxo oxidoreductases (EC 1.2)

1.2.1 - NAD or NADP acceptor	Aldehyde dehydrogenase: Acetaldehyde dehydrogenase (ALDH2) - Long-chain-aldehyde dehydrogenase Glyceraldehyde 3-phosphate dehydrogenase

1.2.4 - disulfide acceptor	Oxoglutarate dehydrogenase - Pyruvate dehydrogenase - Branched-chain alpha-keto acid dehydrogenase complex

v • d • e

Metabolism: amino acid metabolism - synthesis and catabolism enzymes (essential in CAPS)

K→acetyl-CoA

G→pyruvate

glycine→serine→	Serine hydroxymethyltransferase - Serine dehydratase

alanine→	Alanine transaminase

cysteine→	D-cysteine desulfhydrase

threonine→	L-threonine dehydrogenase

G→glutamate


HISTIDINE→	Histidine ammonia-lyase - Urocanate hydratase - Formiminotransferase cyclodeaminase

proline→	Proline oxidase - Pyrroline-5-carboxylate reductase - 1-Pyrroline-5-carboxylate dehydrogenase/ALDH4A1 - PYCR1

arginine→	Ornithine aminotransferase - Ornithine decarboxylase - Agmatinase

→alpha-ketoglutarate→TCA	Glutamate dehydrogenase

G→propionyl-CoA

G→fumarate


PHENYLALANINE→tyrosine→	Phenylalanine hydroxylase - Tyrosine aminotransferase - 4-Hydroxyphenylpyruvate dioxygenase - Homogentisate 1,2-dioxygenase - Fumarylacetoacetate hydrolase