甲基丙二酸單醯輔酶A變位酶

甲基丙二酸單醯輔酶A變位酶
命名
系統命名
縮寫
識別碼
EC編號	5.4.99.2
CAS號	9023-90-9
資料庫
IntEnz	IntEnz瀏覽
BRENDA（英語：BRENDA）	BRENDA入口
ExPASy（英語：ExPASy）	NiceZyme瀏覽
KEGG	KEGG入口
MetaCyc（英語：MetaCyc）	代謝路徑
PRIAM（英語：PRIAM_enzyme-specific_profiles）	概述
PDB	RCSB PDB PDBj PDBe PDBsum
基因本體	AmiGO / EGO
搜索
PMC	相關文獻
PubMed	相關文獻

甲基丙二酸單醯輔酶A變位酶
	Rendering based on PDB 2XIJ.
有效結構
PDB	直系同源檢索：PDBe, RCSB
PDB查詢代碼列表
	2XIJ, 2XIQ, 3BIC
標識
代號	MUT; MCM
擴展標識	遺傳學：609058 鼠基因：97239 同源基因：20097 GeneCards: MUT Gene
EC編號	5.4.99.2
基因本體論描述
分子功能	· methylmalonyl-CoA mutase activity; · cobalamin binding; · metal ion binding; · modified amino acid binding;
細胞成分	· mitochondrion; · mitochondrial matrix;
生物過程	· fatty acid beta-oxidation; · post-embryonic development; · short-chain fatty acid catabolic process; · cellular lipid metabolic process; · small molecule metabolic process; · homocysteine metabolic process;
	Sources: Amigo / QuickGO
RNA表達模式
	更多表達數據
直系同源體
	閱; 論; 編;

甲基丙二酸單醯輔酶A變位酶（英語：Methylmalonyl Coenzyme-A mutase，MCM，亦簡稱甲基丙二醯輔酶A變位酶）是一種在代謝途徑上將甲基丙二酸單醯輔酶A轉換為琥珀醯輔酶A的酶，同時需要維生素B₁₂的幫助。

功能[編輯]

甲基丙二醯輔酶A變位酶主要分布在粒線體中，催化甲基丙二醯輔酶A異構為琥珀醯輔酶A從而進入三羧酸循環。而甲基丙二醯輔酶A來源於丙醯輔酶A，後者是異亮氨酸、纈氨酸、蘇氨酸、甲硫氨酸、胸腺嘧啶、膽固醇以及奇數鏈脂肪酸分解代謝的共同中間體。

人類基因組[編輯]

人類基因組中編碼該酶的基因縮寫為MUT。^[1]

參考文獻[編輯]

^ Entrez Gene: MUT methylmalonyl Coenzyme A mutase. （原始內容存檔於2010-04-12）.

延伸閱讀[編輯]

Ledley FD, Rosenblatt DS. Mutations in mut methylmalonic acidemia: clinical and enzymatic correlations.. Hum. Mutat. 1997, 9 (1): 1–6. PMID 8990001. doi:10.1002/(SICI)1098-1004(1997)9:1<1::AID-HUMU1>3.0.CO;2-E.
Ludwig ML, Matthews RG. Structure-based perspectives on B12-dependent enzymes.. Annu. Rev. Biochem. 1997, 66: 269–313. PMID 9242908. doi:10.1146/annurev.biochem.66.1.269.
Lubrano R, Elli M, Rossi M; et al. Renal transplant in methylmalonic acidemia: could it be the best option? Report on a case at 10 years and review of the literature.. Pediatr. Nephrol. 2007, 22 (8): 1209–14. PMID 17401587. doi:10.1007/s00467-007-0460-z.
Frenkel EP, Kitchens RL. Intracellular localization of hepatic propionyl-CoA carboxylase and methylmalonyl-CoA mutase in humans and normal and vitamin B12 deficient rats.. Br. J. Haematol. 1978, 31 (4): 501–13. PMID 24458. doi:10.1111/j.1365-2141.1975.tb00885.x.
Crane AM, Jansen R, Andrews ER, Ledley FD. Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria.. J. Clin. Invest. 1992, 89 (2): 385–91. PMC 442864 . PMID 1346616. doi:10.1172/JCI115597.
Crane AM, Martin LS, Valle D, Ledley FD. Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase.. Hum. Genet. 1992, 89 (3): 259–64. PMID 1351030. doi:10.1007/BF00220536.
Raff ML, Crane AM, Jansen R; et al. Genetic characterization of a MUT locus mutation discriminating heterogeneity in mut0 and mut- methylmalonic aciduria by interallelic complementation.. J. Clin. Invest. 1991, 87 (1): 203–7. PMC 295026 . PMID 1670635. doi:10.1172/JCI114972.
Jansen R, Ledley FD. Heterozygous mutations at the mut locus in fibroblasts with mut0 methylmalonic acidemia identified by polymerase-chain-reaction cDNA cloning.. Am. J. Hum. Genet. 1990, 47 (5): 808–14. PMC 1683687 . PMID 1977311.
Nham SU, Wilkemeyer MF, Ledley FD. Structure of the human methylmalonyl-CoA mutase (MUT) locus.. Genomics. 1991, 8 (4): 710–6. PMID 1980486. doi:10.1016/0888-7543(90)90259-W.
Ledley FD, Lumetta M, Nguyen PN; et al. Molecular cloning of L-methylmalonyl-CoA mutase: gene transfer and analysis of mut cell lines.. Proc. Natl. Acad. Sci. U.S.A. 1988, 85 (10): 3518–21. PMC 280243 . PMID 2453061. doi:10.1073/pnas.85.10.3518.
Jansen R, Kalousek F, Fenton WA; et al. Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction.. Genomics. 1989, 4 (2): 198–205. PMID 2567699. doi:10.1016/0888-7543(89)90300-5.
Fenton WA, Hack AM, Kraus JP, Rosenberg LE. Immunochemical studies of fibroblasts from patients with methylmalonyl-CoA mutase apoenzyme deficiency: detection of a mutation interfering with mitochondrial import.. Proc. Natl. Acad. Sci. U.S.A. 1987, 84 (5): 1421–4. PMC 304442 . PMID 2881300. doi:10.1073/pnas.84.5.1421.
Zoghbi HY, O'Brien WE, Ledley FD. Linkage relationships of the human methylmalonyl CoA mutase to the HLA and D6S4 loci on chromosome 6.. Genomics. 1989, 3 (4): 396–8. PMID 2907507. doi:10.1016/0888-7543(88)90135-8.
Kolhouse JF, Utley C, Allen RH. Isolation and characterization of methylmalonyl-CoA mutase from human placenta.. J. Biol. Chem. 1980, 255 (7): 2708–12. PMID 6102092.
Fenton WA, Hack AM, Willard HF; et al. Purification and properties of methylmalonyl coenzyme A mutase from human liver.. Arch. Biochem. Biophys. 1982, 214 (2): 815–23. PMID 6124211. doi:10.1016/0003-9861(82)90088-1.
Qureshi AA, Crane AM, Matiaszuk NV; et al. Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria.. J. Clin. Invest. 1994, 93 (4): 1812–9. PMC 294249 . PMID 7909321. doi:10.1172/JCI117166.
Crane AM, Ledley FD. Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia.. Am. J. Hum. Genet. 1994, 55 (1): 42–50. PMC 1918235 . PMID 7912889.
Janata J, Kogekar N, Fenton WA. Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation.. Hum. Mol. Genet. 1998, 6 (9): 1457–64. PMID 9285782. doi:10.1093/hmg/6.9.1457.

外部連結[編輯]

[entrez-1] Entrez Gene: MUT methylmalonyl Coenzyme A mutase. （原始內容存檔於2010-04-12）.

[1]