Molecular Target Synopsis
Overview
Domains and Structures
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Ligand Efficiency Plot
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pam (Q68G84) - Overview - Molecular Target Synopsis

Protein


pam, Phenylalanine aminomutase (L-beta-phenylalanine forming)
Enzyme Classification 5.4.3.10
UniProt Q68G84

Also Known as PAM_TAXWC, pam

Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate. Homodimer (PubMed:15878763). Homotetramer, dimer of dimers (PubMed:24786474).

4V2R
IRONING OUT THEIR DIFFERENCES: DISSECTING THE STRUCTURAL DETERMINANTS OF A PHENYLALANINE AMINOMUTASE AND AMMONIA LYASE
RCSB/PDB
Inspect Structure
See all 3D Structures for pam

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
687Q68G84-1

Sub-cellular localization


UniProt: pam is active in the following subcellular-locations: cytoplasm.
GO terms: pam is active in the following subcellular-locations: cytoplasm.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project pam has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For pam there are:
10 structures (36 chains) solved
8 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis