aspartate-semialdehyde dehydrogenase

アスパラギン酸セミアルデヒド脱水素酵素、アスパラギン酸セミアルデヒドデヒドロゲナーゼ

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/18 00:50:49」(JST)

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aspartate-semialdehyde dehydrogenase
Identifiers
EC number	1.2.1.11
CAS number	9000-98-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it.

The enzyme catalyzes the reversible chemical reaction

L-aspartate 4-semialdehyde + phosphate + NADP⁺ L-4-aspartyl phosphate + NADPH + H⁺

The 3 substrates of this enzyme are L-aspartate 4-semialdehyde, phosphate, and NADP⁺, whereas its 3 products are L-4-aspartyl phosphate, NADPH, and H⁺. In physiological conditions however, the reaction runs in the opposite direction. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating). Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta-semialdehyde:NADP+ oxidoreductase, (phosphorylating), aspartic beta-semialdehyde dehydrogenase, and ASA dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism and lysine biosynthesis.

Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5' UTR of some Asd genes.

Protein families

Semialdehyde dehydrogenase, dimerisation domain
Identifiers
Symbol	Semialdhyde_dhC
Pfam	PF02774
Pfam clan	CL0139
InterPro	IPR012280
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

This domain contains both N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. It also contains the yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acetyl-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a dimerisation domain of semialdehyde dehydrogenase.

Structural studies

As of late 2007, 24 structures have been solved for this class of enzymes, with PDB accession codes 1BRM, 1GL3, 1MB4, 1MC4, 1NWC, 1NWH, 1NX6, 1OZA, 1PQP, 1PQU, 1PR3, 1PS8, 1PU2, 1Q2X, 1T4B, 1T4D, 1TA4, 1TB4, 1YS4, 2EP5, 2GYY, 2GZ1, 2GZ2, and 2GZ3.

References

• BLACK S, WRIGHT NG (1955). "Aspartic beta-semialdehyde dehydrogenase and aspartic beta-semialdehyde". J. Biol. Chem. 213 (1): 39–50. PMID 14353904. 
• Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.

UpToDate Contents

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• 1. グルコース-6-リン酸脱水素酵素欠損症の遺伝学および病態生理 genetics and pathophysiology of glucose 6 phosphate dehydrogenase deficiency
• 2. 先天性代謝異常：代謝性救急疾患 inborn errors of metabolism metabolic emergencies
• 3. 成人における肝性脳症：治療 hepatic encephalopathy in adults treatment
• 4. 肝細胞障害を検出するための肝臓生化学検査 liver biochemical tests that detect injury to hepatocytes
• 5. HELLP症候群 hellp syndrome

English Journal

• Accumulation of a threonine biosynthetic intermediate attenuates general amino acid control by accelerating degradation of Gcn4 via Pho85 and Cdk8.

• Rawal Y, Qiu H, Hinnebusch AG.
• PLoS genetics.PLoS Genet.2014 Jul 31;10(7):e1004534. doi: 10.1371/journal.pgen.1004534. eCollection 2014.
• Gcn4 is a master transcriptional regulator of amino acid and vitamin biosynthetic enzymes subject to the general amino acid control (GAAC), whose expression is upregulated in response to amino acid starvation in Saccharomyces cerevisiae. We found that accumulation of the threonine pathway intermedia
• PMID 25079372

• Shape-based virtual screening, docking, and molecular dynamics simulations to identify Mtb-ASADH inhibitors.

• Kumar R1, Garg P, Bharatam PV.
• Journal of biomolecular structure & dynamics.J Biomol Struct Dyn.2014 Jun 23:1-12. [Epub ahead of print]
• Aspartate β-semialdehyde dehydrogenase (ASADH) is a key enzyme for the biosynthesis of essential amino acids and several important metabolites in microbes. Inhibition of ASADH enzyme is a promising drug target strategy against Mycobacterium tuberculosis (Mtb). In this work, in silico approach was u
• PMID 24875451

• Evaluation of efficacy, biodistribution and safety of antibiotic-free plasmid encoding somatostatin genes delivered by attenuated Salmonella enterica serovar Choleraesuis.

• Liang A1, Riaz H1, Dong F1, Luo X1, Yu X1, Han Y1, Chong Z1, Han L2, Guo A2, Yang L3.
• Vaccine.Vaccine.2014 Mar 10;32(12):1368-74. doi: 10.1016/j.vaccine.2014.01.026. Epub 2014 Jan 30.
• We describe here a balanced-lethal system using an Asd(+) expression plasmid pVGS/2SS-asd encoding two copies of somatostatin (SS) genes carried by Δasd/Δcrp double mutant Salmonella enterica serovar Choleraesuis (named C501). The advantage of this novel system is the use of asd (aspartate-semiald
• PMID 24486312

Japanese Journal

• Isolation and characterization of the aspartate kinase and aspartate semialdehyde dehydrogenase ope-ron from mycobacteria.

• CIRLLO J. D.
• Mol. Microbiol. 11, 629-639, 1994
• NAID 30014458909

Related Links

• Aspartate-semialdehyde dehydrogenase - Wikipedia, the free ...

In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic ...

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リンク元	「アスパラギン酸セミアルデヒド脱水素酵素」
関連記事	「aspartate」「dehydrogenase」「dehydrogenases」

「アスパラギン酸セミアルデヒド脱水素酵素」

　　[★]

英

aspartate-semialdehyde dehydrogenase

関

アスパラギン酸セミアルデヒドデヒドロゲナーゼ

「aspartate」

　　[★] アスパラギン酸、アスパラギン酸塩

関

Asp、aspartic、aspartic acid、D、L-aspartate、L-aspartic acid、magnesium aspartate、potassium aspartate

aspartic acid

「dehydrogenase」

　　[★] 脱水素酵素 デヒドロゲナーゼ

「dehydrogenases」

　　[★] 脱水素酵素 デヒドロゲナーゼ