甲基丙二酸单酰辅酶A变位酶

甲基丙二酸单酰辅酶A变位酶
命名
系统命名
缩写
识别码
EC編號	5.4.99.2
CAS号	9023-90-9
数据库
IntEnz	IntEnz浏览
BRENDA（英语：BRENDA）	BRENDA入口
ExPASy（英语：ExPASy）	NiceZyme浏览
KEGG	KEGG入口
MetaCyc（英语：MetaCyc）	代谢路径
PRIAM（英语：PRIAM_enzyme-specific_profiles）	概述
PDB	RCSB PDB PDBj PDBe PDBsum
基因本体	AmiGO / EGO
搜索
PMC	相关文献
PubMed	相关文献

甲基丙二酸单酰辅酶A变位酶
甲基丙二酸单酰辅酶A变位酶
	Rendering based on PDB 2XIJ.
有效结构
PDB	直系同源检索：PDBe, RCSB
PDB查询代码列表
	2XIJ, 2XIQ, 3BIC
标识
代号	MUT; MCM
扩展标识	遗传学：609058 鼠基因：97239 同源基因：20097 GeneCards: MUT Gene
EC編號	5.4.99.2
基因本体论描述
分子功能	· methylmalonyl-CoA mutase activity; · cobalamin binding; · metal ion binding; · modified amino acid binding;
细胞成分	· mitochondrion; · mitochondrial matrix;
生物过程	· 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表达模式
	更多表达数据
直系同源体
物种	人类
Entrez	4594
Ensembl	ENSG00000146085
UniProt	P22033
mRNA序列	NM_000255
蛋白序列	NP_000246
基因位置	Chr 6:; 49.4 – 49.43 Mb
PubMed查询	[1]
	查; 论; 编;

甲基丙二酸单酰辅酶A变位酶（英語：Methylmalonyl Coenzyme-A mutase，MCM，亦简称甲基丙二酰辅酶A变位酶）是一种在代谢途径上将甲基丙二酸单酰辅酶A转换为琥珀酰辅酶A的酶，同时需要维生素B₁₂的帮助。

功能

甲基丙二酰辅酶A变位酶主要分布在线粒体中，催化甲基丙二酰辅酶A异构为琥珀酰辅酶A从而进入三羧酸循环。而甲基丙二酰辅酶A来源于丙酰辅酶A，后者是异亮氨酸、缬氨酸、苏氨酸、甲硫氨酸、胸腺嘧啶、胆固醇以及奇数链脂肪酸分解代谢的共同中间体。

人类基因组

人类基因组中编码该酶的基因缩写为MUT。^[1]

参考文献

^ Entrez Gene: MUT methylmalonyl Coenzyme A mutase. （原始内容存档于2010-04-12）.

延伸阅读

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.

外部链接

[entrez-1] Entrez Gene: MUT methylmalonyl Coenzyme A mutase. （原始内容存档于2010-04-12）.

[1]

甲基丙二酸单酰辅酶A变位酶

功能

人类基因组

参考文献

延伸阅读

外部链接

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