3-イソプロピルリンゴ酸脱水素酵素、3-イソプロピルリンゴ酸デヒドロゲナーゼ
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/11/06 00:34:32」(JST)
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| 3-Isopropylmalate dehydrogenase |
| Identifiers |
| EC number |
1.1.1.85 |
| CAS number |
9030-97-1 |
| 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 |
|
3-Isopropylmalate dehydrogenase (EC 1.1.1.85) is an enzyme that catalyzes the chemical reactions[1][2][3][4]
- (2R,3S)-3-isopropylmalate + NAD+ 4-methyl-2-oxopentanoate + CO2 + NADH
- (2R,3S)-3-isopropylmalate + NAD+ (2S)-2-isopropyl-3-oxosuccinate + H+ + NADH
- (2S)-2-isopropyl-3-oxosuccinate + H+ 4-methyl-2-oxopentanoate + CO2
References
- ^ Burns RO, Umbarger HE, Gross, SR (1963). "The biosynthesis of leucine. III. The conversion of α-hydroxy-β-carboxyisocaproate to α-ketoisocaproate.". Biochemistry 2: 1053–8. doi:10.1021/bi00905a024. PMID 14087358.
- ^ Calvo JM, Stevens CM, Kalyanpur MG, Umbarger HE (December 1964). "The Absolute Configuration of α-carboxyisocaproic Acid (3-Isopropylmalic Acid), an Intermediate in Leucine Biosynthesis". Biochemistry 3: 2024–7. doi:10.1021/bi00900a043. PMID 14269331.
- ^ Parsons SJ, Burns RO (February 1969). "Purification and Properties of β-Isopropylmalate Dehydrogenase". J. Biol. Chem. 244 (3): 996–1003. PMID 4889950.
- ^ Németh A, Svingor A, Pócsik M, Dobó J, Magyar C, Szilágyi A, Gál P, Závodszky P (February 2000). "Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase". FEBS Lett. 468 (1): 48–52. doi:10.1016/S0014-5793(00)01190-X. PMID 10683439.
English Journal
- Targeted quantitative proteomic investigation employing multiple reaction monitoring on quantitative changes in proteins that regulate volatile biosynthesis of strawberry fruit at different ripening stages.
- Song J1, Du L2, Li L3, Palmer LC4, Forney CF4, Fillmore S4, Zhang Z2, Li X3.
- Journal of proteomics.J Proteomics.2015 Aug 3;126:288-95. doi: 10.1016/j.jprot.2015.06.004. Epub 2015 Jun 15.
- A targeted quantitative proteomic investigation employing the multiple reaction monitoring (MRM, SRM) technique was conducted on strawberry fruit at different development stages. We investigated 22 proteins and isoforms from 32 peptides with 111 peptide transitions, which may be involved in the vola
- PMID 26087350
- Tel1(ATM)-mediated interference suppresses clustered meiotic double-strand-break formation.
- Garcia V1, Gray S1, Allison RM1, Cooper TJ1, Neale MJ1.
- Nature.Nature.2015 Apr 2;520(7545):114-8. doi: 10.1038/nature13993. Epub 2015 Jan 5.
- Meiotic recombination is a critical step in gametogenesis for many organisms, enabling the creation of genetically diverse haploid gametes. In each meiotic cell, recombination is initiated by numerous DNA double-strand breaks (DSBs) created by Spo11, the evolutionarily conserved topoisomerase-like p
- PMID 25539084
- Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.
- Gráczer É1, Palló A2, Oláh J3, Szimler T1, Konarev PV4, Svergun DI4, Merli A5, Závodszky P1, Weiss MS6, Vas M7.
- FEBS letters.FEBS Lett.2015 Jan 16;589(2):240-5. doi: 10.1016/j.febslet.2014.12.005. Epub 2014 Dec 10.
- The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced (∼1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4 kcal/mol increase in the activation energy of the catalysed reaction upon this mutation could also be
- PMID 25497013
Japanese Journal
- Piezo-Adapted 3-Isopropylmalate Dehydrogenase of the Obligate Piezophile Shewanella benthica DB21MT-2 Isolated from the 11,000-m Depth of the Mariana Trench
- KASAHARA Ryota,SATO Takako,TAMEGAI Hideyuki,KATO Chiaki
- Bioscience, biotechnology, and biochemistry 73(11), 2541-2543, 2009-11-23
- … 3-Isopropylmalate dehydrogenase (IPMDH)-encoding <I>leuB</I> …
- NAID 10027548279
- 27 β-脱炭酸脱水素酵素の阻害剤設計(口頭発表の部)
- 江口 正,山本 崇史,南後 恵理子,熊坂 崇
- 天然有機化合物討論会講演要旨集 (50), 185-190, 2008-09-01
- … Homoisocitrate dehydrogenase (HICDH) and 3-isopropylmalate dehydrogenase (IPMDH) belong to a unique family of bifunctional decarboxylating dehydrogenases. … IPMDH is a key enzyme in L-leucine biosynthesis of microorganism and plants, and catalyzes the NAD^+ dependent oxidative decarboxylation of the substrate 3-isopropylmalate to 2-oxoisocaproate. …
- NAID 110007066648
- 1P083 酵素の高温適応化と低温適応化-レイソプロピルリンゴ酸脱水素酵素を例に(蛋白質(蛋白質工学・進化工学)、核酸結合蛋白質、核酸,口頭発表,第45回日本生物物理学会年会)
- 佐々木 道香,林 清香,宇野 真由美,渡辺 敬子,赤沼 哲史,山岸 明彦
- 生物物理 47(SUPPLEMENT_1), S44, 2007-11-20
- NAID 110006561380
Related Links
- Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. ... <p>Describes the metabolic pathway(s ...
- 3-isopropylmalate dehydrogenase Gene leuB Organism Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) Sequence features View only features (sites, domains, PTMs ...) Status Reviewed- - i ...
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脱水素酵素 デヒドロゲナーゼ
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脱水素酵素 デヒドロゲナーゼ