人 METAP1D 抗体对
01AB02859
Methionyl aminopeptidase type 1D, mitochondrial (METAP1D) is a nuclear-encoded mitochondrial metalloprotease that functions in the essential N-terminal methionine excision pathway. It catalyzes the removal of the N-terminal methionine from nascent polypeptides, particularly when the second residue is small and uncharged, such as alanine, glycine, or serine. This enzymatic activity is dependent on the prior deformylation of the initiator methionine and is critical for proper protein maturation, stability, and mitochondrial protein homeostasis. As a member of the M24A peptidase family, METAP1D plays a vital role in preserving myogenic cell integrity by regulating mitochondrial content and activity. Its role in substrate recognition and catalytic efficiency is essential for the maintenance of the mitochondrial proteome.
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技术参数
- 靶点基因名
- METAP1D
- 基因别名
- MAP1D
- 蛋白别名
- methionyl aminopeptidase type 1D, mitochondrial; METAP1D
- UniProt
- Q6UB28
- 物种
- Human
产品详情
- 靶点名称
- METAP1D
- 蛋白名称
- methionyl aminopeptidase type 1D, mitochondrial
- 蛋白别名
- Methionine aminopeptidase 1D; mitochondrial; MAP 1D; MetAP 1D; Methionyl aminopeptidase type 1D; mitochondrial; Peptidase M 1D
- 靶点基因名
- METAP1D
- 基因别名
- MAP1D
- UniProt
- Q6UB28
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Methionyl aminopeptidase type 1D, mitochondrial (METAP1D) is a nuclear-encoded mitochondrial metalloprotease that functions in the essential N-terminal methionine excision pathway. It catalyzes the removal of the N-terminal methionine from nascent polypeptides, particularly when the second residue is small and uncharged, such as alanine, glycine, or serine. This enzymatic activity is dependent on the prior deformylation of the initiator methionine and is critical for proper protein maturation, stability, and mitochondrial protein homeostasis. As a member of the M24A peptidase family, METAP1D plays a vital role in preserving myogenic cell integrity by regulating mitochondrial content and activity. Its role in substrate recognition and catalytic efficiency is essential for the maintenance of the mitochondrial proteome.