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Q68G84

- PAM_TAXWC

UniProt

Q68G84 - PAM_TAXWC

Protein

Phenylalanine aminomutase (L-beta-phenylalanine forming)

Gene

pam

Organism
Taxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first commited 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.3 Publications

    Catalytic activityi

    L-phenylalanine = L-beta-phenylalanine.
    L-phenylalanine = trans-cinnamate + ammonia.

    Kineticsi

    1. KM=1.1 mM for L-Phe2 Publications

    Vmax=110 µmol/min/mg enzyme with L-Phe as substrate2 Publications

    pH dependencei

    Optimum pH is 7.5-8.0.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei80 – 801Proton donor/acceptor2 Publications
    Binding sitei231 – 2311Substrate
    Binding sitei319 – 3191Substrate
    Binding sitei325 – 3251Substrate
    Binding sitei355 – 3551Substrate
    Binding sitei458 – 4581Substrate

    GO - Molecular functioni

    1. intramolecular transferase activity, transferring amino groups Source: UniProtKB
    2. phenylalanine ammonia-lyase activity Source: UniProtKB-EC

    GO - Biological processi

    1. alkaloid biosynthetic process Source: UniProtKB
    2. L-phenylalanine catabolic process Source: InterPro
    3. L-phenylalanine metabolic process Source: UniProtKB
    4. paclitaxel biosynthetic process Source: UniProtKB
    5. phenylpropanoid metabolic process Source: UniProtKB-KW
    6. protein homotetramerization Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Biological processi

    Alkaloid metabolism, Phenylpropanoid metabolism, Taxol biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00713; UER00725.
    UPA00842.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine aminomutase (L-beta-phenylalanine forming) (EC:5.4.3.10)
    Alternative name(s):
    Phenylalanine ammonia-lyase (EC:4.3.1.24)
    Gene namesi
    Name:pam
    OrganismiTaxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis)
    Taxonomic identifieri29808 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesTaxaceaeTaxus

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Biotechnological usei

    Could be used for the stereoselective biosynthesis of beta-amino acids via amination of cinnamic acid derivatives.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801Y → A or F: Abolishes enzyme activity. 1 Publication
    Mutagenesisi231 – 2311N → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity. 2 Publications
    Mutagenesisi231 – 2311N → X: Abolishes enzyme activity; when associated with X-355. 2 Publications
    Mutagenesisi319 – 3191Q → M: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with K-325. 1 Publication
    Mutagenesisi322 – 3221Y → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity. 2 Publications
    Mutagenesisi322 – 3221Y → X: Abolishes enzyme activity; when associated with X-371. 2 Publications
    Mutagenesisi325 – 3251R → K: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with M-319. 1 Publication
    Mutagenesisi355 – 3551N → X: Abolishes enzyme activity; when associated with X-231. 1 Publication
    Mutagenesisi371 – 3711F → X: Abolishes enzyme activity; when associated with X-322. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 687687Phenylalanine aminomutase (L-beta-phenylalanine forming)PRO_0000429970Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki175 ↔ 1775-imidazolinone (Ala-Gly)
    Modified residuei176 – 17612,3-didehydroalanine (Ser)

    Post-translational modificationi

    Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.

    Interactioni

    Subunit structurei

    Homodimer (PubMed:15878763). Homotetramer, dimer of dimers (PubMed:24786474).2 Publications

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YIIX-ray2.18A/B/C/D1-687[»]
    4BAAX-ray2.50A/B/C/D1-687[»]
    4BABX-ray2.56A/B/C/D1-687[»]
    ProteinModelPortaliQ68G84.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PAL/histidase family.Curated

    Family and domain databases

    Gene3Di1.10.274.20. 1 hit.
    1.10.275.10. 1 hit.
    InterProiIPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    IPR005922. Phe_NH3-lyase.
    IPR023144. Phe_NH3-lyase_shielding_dom.
    [Graphical view]
    PfamiPF00221. Lyase_aromatic. 1 hit.
    [Graphical view]
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
    PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q68G84-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFAVESRSH VKDILGLINA FNEVKKITVD GTTPITVAHV AALARRHDVK    50
    VALEAEQCRA RVETCSSWVQ RKAEDGADIY GVTTGFGACS SRRTNRLSEL 100
    QESLIRCLLA GVFTKGCAPS VDELPATATR SAMLLRLNSF TYGCSGIRWE 150
    VMEALEKLLN SNVSPKVPLR GSVSASGDLI PLAYIAGLLI GKPSVIARIG 200
    DDVEVPAPEA LSRVGLRPFK LQAKEGLALV NGTSFATAVA STVMYDANVL 250
    LLLVETLCGM FCEVIFGREE FAHPLIHKVK PHPGQIESAE LLEWLLRSSP 300
    FQELSREYYS IDKLKKPKQD RYALRSSPQW LAPLVQTIRD ATTTVETEVN 350
    SANDNPIIDH ANDRALHGAN FQGSAVGFYM DYVRIAVAGL GKLLFAQFTE 400
    LMIEYYSNGL PGNLSLGPDL SVDYGLKGLD IAMAAYSSEL QYLANPVTTH 450
    VHSAEQHNQD INSLALISAR KTEEALDILK LMIASHLTAM CQAVDLRQLE 500
    EALVKVVENV VSTLADECGL PNDTKARLLY VAKAVPVYTY LESPCDPTLP 550
    LLLGLKQSCF DTILALHKKD GIETDTLVDR LAEFEKRLSD RLENEMTAVR 600
    VLYEKKGHKT ADNNDALVRI QGSKFLPFYR FVREELDTGV MSARREQTPQ 650
    EDVQKVFDAI ADGRITVPLL HCLQGFLGQP NGCANGV 687
    Length:687
    Mass (Da):75,332
    Last modified:October 11, 2004 - v1
    Checksum:iD9BC13C7C689A421
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY724735 mRNA. Translation: AAU01182.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY724735 mRNA. Translation: AAU01182.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YII X-ray 2.18 A/B/C/D 1-687 [» ]
    4BAA X-ray 2.50 A/B/C/D 1-687 [» ]
    4BAB X-ray 2.56 A/B/C/D 1-687 [» ]
    ProteinModelPortali Q68G84.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00713 ; UER00725 .
    UPA00842 .

    Family and domain databases

    Gene3Di 1.10.274.20. 1 hit.
    1.10.275.10. 1 hit.
    InterProi IPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    IPR005922. Phe_NH3-lyase.
    IPR023144. Phe_NH3-lyase_shielding_dom.
    [Graphical view ]
    Pfami PF00221. Lyase_aromatic. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR01226. phe_am_lyase. 1 hit.
    PROSITEi PS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, cloning, and functional expression of phenylalanine aminomutase: the first committed step in Taxol side-chain biosynthesis."
      Steele C.L., Chen Y., Dougherty B.A., Li W., Hofstead S., Lam K.S., Xing Z., Chiang S.J.
      Arch. Biochem. Biophys. 438:1-10(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    2. "Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-regioselective asymmetric amination of cinnamates."
      Wu B., Szymanski W., Wybenga G.G., Heberling M.M., Bartsch S., de Wildeman S., Poelarends G.J., Feringa B.L., Dijkstra B.W., Janssen D.B.
      Angew. Chem. Int. Ed. 51:482-486(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, MUTAGENESIS OF ASN-231; GLN-319; TYR-322; ARG-325; ASN-355 AND PHE-371, ACTIVE SITE, PTM.
    3. "Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from Taxus chinensis."
      Wybenga G.G., Szymanski W., Wu B., Feringa B.L., Janssen D.B., Dijkstra B.W.
      Biochemistry 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH TRANS-CINNAMATE, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, PTM, SUBUNIT, MUTAGENESIS OF TYR-80; ASN-231 AND TYR-322.

    Entry informationi

    Entry nameiPAM_TAXWC
    AccessioniPrimary (citable) accession number: Q68G84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 3, 2014
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3