PAM report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0010043Biological processresponse to zinc ion
GO_0001519Biological processpeptide amidation
GO_0062112Biological processfatty acid primary amide biosynthetic process
GO_0030667Cellular componentsecretory granule membrane
GO_0030658Cellular componenttransport vesicle membrane
GO_0070062Cellular componentextracellular exosome
GO_0005576Cellular componentextracellular region
GO_0016020Cellular componentmembrane
GO_0004598Molecular functionpeptidylamidoglycolate lyase activity
GO_0005507Molecular functioncopper ion binding
GO_0005509Molecular functioncalcium ion binding
GO_0004504Molecular functionpeptidylglycine monooxygenase activity
GO_0005515Molecular functionprotein binding
GO_0031418Molecular functionL-ascorbic acid binding
GO_0008270Molecular functionzinc ion binding

IV. Literature review

[source]
Gene namePAM
Protein namePeptidylglycine alpha-amidating monooxygenase
Peptidyl-glycine alpha-amidating monooxygenase (PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase (PHM) (EC 1.14.17.3); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5) (Peptidylamidoglycolate lyase) (PAL)]
peptidylamidoglycolate lyase (EC 4.3.2.5)
Synonyms
DescriptionFUNCTION: Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides . Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate . The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate . Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity). .

AccessionsA0A804HK31
ENST00000438793.8 [P19021-1]
ENST00000512073.1
A0A804HKM7
A0A804HJJ2
ENST00000506006.1
ENST00000682972.1
F8W8D9
H0Y9I4
D6RAQ2
ENST00000511839.5
ENST00000684529.1 [P19021-5]
ENST00000682407.1 [P19021-6]
ENST00000509523.2
ENST00000345721.6
ENST00000505654.1
ENST00000379799.7
ENST00000455264.7 [P19021-3]
A0A804HLJ2
ENST00000346918.7 [P19021-4]
ENST00000348126.7 [P19021-2]
D6RF09
A0A804HIQ0
D6RCD5
Q7KYY0
A0A8C8KD64
ENST00000684043.1
P19021
ENST00000509832.5
ENST00000510208.2
D6RG20
A0A804HKV8
ENST00000504456.1
D6R961
A0A804HI59
ENST00000510006.6
H7BYD9
ENST00000684379.1
ENST00000682024.1
D6RDU2
ENST00000511477.5
ENST00000504691.1
ENST00000682882.1
ENST00000304400.12
A0A804HLE0