人 PAM 抗体对
01AB04122
Peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional enzyme crucial for the biosynthesis of many signaling peptides and fatty acid amides. It catalyzes the conversion of peptides with a C-terminal glycine into peptides with a terminal amide group, a process essential for the bioactivity of these peptides. PAM has two enzymatically active domains: peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). The PHM domain hydroxylates the C-terminal glycine residue using a copper ion cofactor and oxygen, while the PAL domain completes the conversion by eliminating glyoxylate from the hydroxylated glycine, producing the alpha-amidated peptide. This enzyme is encoded by the PAM gene in humans and is expressed in various endocrine and exocrine glands. The transformation makes peptides more hydrophobic and neutrally charged, enhancing their ability to bind to receptors.
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技术参数
- 靶点基因名
- PAM
- 蛋白别名
- peptidylglycine alpha-amidating monooxygenase; PAM
- UniProt
- P19021
- 物种
- Human
产品详情
- 靶点名称
- PAM
- 蛋白名称
- peptidylglycine alpha-amidating monooxygenase
- 蛋白别名
- Peptidyl-glycine alpha-amidating monooxygenase; PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase; PHM; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; Peptidylamidoglycolate lyase; PAL]
- 靶点基因名
- PAM
- UniProt
- P19021
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional enzyme crucial for the biosynthesis of many signaling peptides and fatty acid amides. It catalyzes the conversion of peptides with a C-terminal glycine into peptides with a terminal amide group, a process essential for the bioactivity of these peptides. PAM has two enzymatically active domains: peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). The PHM domain hydroxylates the C-terminal glycine residue using a copper ion cofactor and oxygen, while the PAL domain completes the conversion by eliminating glyoxylate from the hydroxylated glycine, producing the alpha-amidated peptide. This enzyme is encoded by the PAM gene in humans and is expressed in various endocrine and exocrine glands. The transformation makes peptides more hydrophobic and neutrally charged, enhancing their ability to bind to receptors.