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Q68G84

- PAM_TAXWC

UniProt

Q68G84 - PAM_TAXWC

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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

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.

Catalytic activityi

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

Kineticsi

  1. KM=1.1 mM for L-Phe

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

pH dependencei

Optimum pH is 7.5-8.0.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801Proton donor/acceptor
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
Complete GO annotation...

GO - Biological processi

  1. L-phenylalanine catabolic process Source: InterPro
  2. L-phenylalanine metabolic process Source: UniProtKB
  3. alkaloid biosynthetic process Source: UniProtKB
  4. cinnamic acid biosynthetic process Source: UniProtKB-UniPathway
  5. paclitaxel biosynthetic process Source: UniProtKB
  6. protein homotetramerization Source: UniProtKB
Complete GO annotation...

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: UniProtKB-SubCell
Complete GO annotation...

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801Y → A or F: Abolishes enzyme activity.
Mutagenesisi231 – 2311N → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity.
Mutagenesisi231 – 2311N → X: Abolishes enzyme activity; when associated with X-355.
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.
Mutagenesisi322 – 3221Y → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity.
Mutagenesisi322 – 3221Y → X: Abolishes enzyme activity; when associated with X-371.
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.
Mutagenesisi355 – 3551N → X: Abolishes enzyme activity; when associated with X-231.
Mutagenesisi371 – 3711F → X: Abolishes enzyme activity; when associated with X-322.

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 (1 Publication). Homotetramer, dimer of dimers (1 Publication).

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.

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...

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: September 3, 2014
This is version 77 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

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