Aldehyde dehydrogenase 4 family, member A1

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Aldehyde dehydrogenase 4 family, member A1

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Aldehyde dehydrogenase 4 family, member A1

Identifiers

Symbols

ALDH4A1; ALDH4; DKFZp779M035; P5CD; P5CDh

External IDs

OMIM: 606811 MGI: 2443883 HomoloGene: 6081 GeneCards: ALDH4A1 Gene

EC number

1.5.1.12

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 metabolic process • proline biosynthetic process • proline catabolic process • cellular nitrogen compound metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
19.2 – 19.23 Mb

Chr 4:
139.18 – 139.21 Mb

PubMed search

[1]

[2]

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ALDH4A1 gene.^[1]^[2]

This protein belongs to the aldehyde dehydrogenase family of proteins. This enzyme is a mitochondrial matrix NAD-dependent dehydrogenase that 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.^[2]

References

^ Hu CA, Lin WW, Valle D (Jun 1996). "Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase". J Biol Chem 271 (16): 9795–800. doi:10.1074/jbc.271.16.9795. PMID 8621661.
^ ^a ^b "Entrez Gene: ALDH4A1 aldehyde dehydrogenase 4 family, member A1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8659.

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. doi:10.1172/JCI109593. PMC 371284. PMID 500817. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=371284.
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. doi:10.1002/elps.11501301201. PMID 1286669.
Goodman SI, Mace JW, Miles BS, et al. (1974). "Defective hydroxyproline metabolism in type II hyperprolinemia.". Biochemical medicine 10 (4): 329–36. doi:10.1016/0006-2944(74)90036-2. 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1093/hmg/7.9.1411. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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.

This article on a gene on chromosome 1 is a stub. You can help Wikipedia by expanding it.

v · d · eAldehyde/oxo oxidoreductases (EC 1.2)

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

1.2.2: cytochrome	Formate dehydrogenase (cytochrome)

1.2.3: oxygen	Aldehyde oxidase

1.2.4: disulfide	Oxoglutarate dehydrogenase · Pyruvate dehydrogenase · Branched-chain alpha-keto acid dehydrogenase complex (BCKDHA, BCKDHB, DBT, DLD)

1.2.7: iron-sulfur protein	Pyruvate synthase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

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

K→acetyl-CoA

G→pyruvate
→citrate

glycine→serine→	Serine hydroxymethyltransferase · Serine dehydratase glycine→creatine: Guanidinoacetate N-methyltransferase · Creatine kinase

alanine→	Alanine transaminase

cysteine→	D-cysteine desulfhydrase

threonine→	L-threonine dehydrogenase

G→glutamate→
α-ketoglutarate

G→propionyl-CoA→
succinyl-CoA

VALINE→	Branched chain aminotransferase · Branched-chain alpha-keto acid dehydrogenase complex · Enoyl-CoA hydratase · 3-hydroxyisobutyryl-CoA hydrolase · 3-hydroxyisobutyrate dehydrogenase · Methylmalonate semialdehyde dehydrogenase

ISOLEUCINE→	Branched chain aminotransferase · Branched-chain alpha-keto acid dehydrogenase complex · 3-hydroxy-2-methylbutyryl-CoA dehydrogenase

METHIONINE→	generation of homocysteine: Methionine adenosyltransferase · Adenosylhomocysteinase regeneration of methionine: Methionine synthase/Homocysteine methyltransferase · Betaine-homocysteine methyltransferase conversion to cysteine: Cystathionine beta synthase · Cystathionine gamma-lyase

THREONINE→	Threonine aldolase

→succinyl-CoA→TCA	Propionyl-CoA carboxylase · Methylmalonyl CoA epimerase · Methylmalonyl-CoA mutase

G→fumarate


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

G→oxaloacetate


asparagine→aspartate→	Asparaginase/Asparagine synthetase · Aspartate transaminase

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

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