Amidating monooxygenase


17-Oct-2020 06:15

The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x x 1. The version number for both the entry and the canonical sequence are also displayed. This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by Uni Prot KB curators or not, in other words, if the entry belongs to the Swiss-Prot section of Uni Prot KB (reviewed) or to the computer-annotated Tr EMBL section (unreviewed). Any medical or genetic information present in this entry is provided for research, educational and informational purposes only.

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Peptidylglycine alpha-amidating monooxygenase (EC 1.14.17.3) is a multifunctional protein containing 2 enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), that act sequentially to catalyze the alpha-amidation of neuroendocrine peptides. Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21.

Human peptidylglycine alpha-amidating monooxygenase: c DNA, cloning and functional expression of a truncated form in COS cells. Genomics 18: 319-321, 1993.[Pub Med: 8288234] [Full Text]" pmid="8288234"Ouafik et al.

(1993) used Southern blot analysis of human placental DNA to demonstrate that PAM is encoded by a single gene. 6: 1571-1584, 1992.[Pub Med: 1448112] [Full Text]" pmid="1448112"Ouafik et al.

By somatic cell hybridization, The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains. (1992) mapped the human PAM gene to the long arm of chromosome 5.

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However Uni Prot KB may contain entries with identical sequences in case of multiple genes (paralogs). Upon integration into Uni Prot KB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’. This subsection of the ‘Entry information’ section shows the date of integration of the entry into Uni Prot KB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’).

Annotation score:2 out of 5 The annotation score provides a heuristic measure of the annotation content of a Uni Prot KB entry or proteome.

This score cannot be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein. This indicates the type of evidence that supports the existence of the protein.

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 (Pub Med:12699694).

Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).

(1990) showed that alternative splicing generates 2 forms of PAM m RNA in humans.



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