PDBsum entry 2ohy

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protein Protein-protein interface(s) links
Lyase, transferase PDB id
Protein chains
526 a.a. *
Waters ×414
* Residue conservation analysis
PDB id:
Name: Lyase, transferase
Title: X-ray crystal structure of tyrosine aminomutase from strepto globisporus
Structure: Tyrosine aminomutase. Chain: a, b. Synonym: ammonia lyase/transferase. Engineered: yes
Source: Streptomyces globisporus. Organism_taxid: 1908. Strain: sgcc4. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.50Å     R-factor:   0.192     R-free:   0.263
Authors: C.Christianson,S.Bruner
Key ref: C.V.Christianson et al. (2007). The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway. Biochemistry, 46, 7205-7214. PubMed id: 17516659 DOI: 10.1021/bi7003685
10-Jan-07     Release date:   12-Jun-07    
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Protein chains
Pfam   ArchSchema ?
Q8GMG0  (Q8GMG0_STRGL) -  MIO-dependent tyrosine 2,3-aminomutase
539 a.a.
526 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: E.C.  - Tyrosine ammonia-lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosine = trans-p-hydroxycinnamate + ammonia
= trans-p-hydroxycinnamate
+ ammonia
      Cofactor: MIO
   Enzyme class 3: E.C.  - Tyrosine 2,3-aminomutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
= 3-amino-3-(4-hydroxyphenyl)propanoate
      Cofactor: MIO
Pyridoxal 5'-phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biosynthetic process   3 terms 
  Biochemical function     catalytic activity     6 terms  


DOI no: 10.1021/bi7003685 Biochemistry 46:7205-7214 (2007)
PubMed id: 17516659  
The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway.
C.V.Christianson, T.J.Montavon, S.G.Van Lanen, B.Shen, S.D.Bruner.
The SgcC4 l-tyrosine 2,3-aminomutase (SgTAM) catalyzes the formation of (S)-beta-tyrosine in the biosynthetic pathway of the enediyne antitumor antibiotic C-1027. SgTAM is homologous to the histidine ammonia lyase family of enzymes whose activity is dependent on the methylideneimidazole-5-one (MIO) cofactor. Unlike the lyase enzymes, SgTAM catalyzes additional chemical transformations resulting in an overall stereospecific 1,2-amino shift in the substrate l-tyrosine to generate (S)-beta-tyrosine. Previously, we provided kinetic, spectroscopic, and mutagenesis data supporting the presence of MIO in the active site of SgTAM [Christenson, S. D.; Wu, W.; Spies, A.; Shen, B.; and Toney, M. D. (2003) Biochemistry 42, 12708-12718]. Here we report the first X-ray crystal structure of an MIO-containing aminomutase, SgTAM, and confirm the structural homology of SgTAM to ammonia lyases. Comparison of the structure of SgTAM to the l-tyrosine ammonia lyase from Rhodobacter sphaeroides provides insight into the structural basis for aminomutase activity. The results show that SgTAM has a closed active site well suited to retain ammonia and minimize the formation of lyase elimination products. The amino acid determinants for substrate recognition and catalysis can be predicted from the structure, setting the framework for detailed mechanistic investigations.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21131229 N.J.Turner (2011).
Ammonia lyases and aminomutases as biocatalysts for the synthesis of α-amino and β-amino acids.
  Curr Opin Chem Biol, 15, 234-240.  
20924508 B.Wu, W.Szymański, H.J.Wijma, C.G.Crismaru, Wildeman, G.J.Poelarends, B.L.Feringa, and D.B.Janssen (2010).
Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase.
  Chem Commun (Camb), 46, 8157-8159.  
20577998 H.A.Cooke, and S.D.Bruner (2010).
Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites.
  Biopolymers, 93, 802-810.
PDB codes: 3kdy 3kdz
20111804 L.Du, and L.Lou (2010).
PKS and NRPS release mechanisms.
  Nat Prod Rep, 27, 255-278.  
20336235 Z.X.Liang (2010).
Complexity and simplicity in the biosynthesis of enediyne natural products.
  Nat Prod Rep, 27, 499-528.  
19123196 B.Wu, W.Szymanski, P.Wietzes, Wildeman, G.J.Poelarends, B.L.Feringa, and D.B.Janssen (2009).
Enzymatic Synthesis of Enantiopure alpha- and beta-Amino Acids by Phenylalanine Aminomutase-Catalysed Amination of Cinnamic Acid Derivatives.
  Chembiochem, 10, 338-344.  
19222035 D.Krug, and R.Müller (2009).
Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF.
  Chembiochem, 10, 741-750.  
19620019 H.A.Cooke, C.V.Christianson, and S.D.Bruner (2009).
Structure and chemistry of 4-methylideneimidazole-5-one containing enzymes.
  Curr Opin Chem Biol, 13, 460-468.  
19246381 S.Lin, S.G.Van Lanen, and B.Shen (2009).
A free-standing condensation enzyme catalyzing ester bond formation in C-1027 biosynthesis.
  Proc Natl Acad Sci U S A, 106, 4183-4188.  
18556022 L.Wang, A.Gamez, H.Archer, E.E.Abola, C.N.Sarkissian, P.Fitzpatrick, D.Wendt, Y.Zhang, M.Vellard, J.Bliesath, S.M.Bell, J.F.Lemontt, C.R.Scriver, and R.C.Stevens (2008).
Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase.
  J Mol Biol, 380, 623-635.  
17918933 S.G.Van Lanen, T.J.Oh, W.Liu, E.Wendt-Pienkowski, and B.Shen (2007).
Characterization of the maduropeptin biosynthetic gene cluster from Actinomadura madurae ATCC 39144 supporting a unifying paradigm for enediyne biosynthesis.
  J Am Chem Soc, 129, 13082-13094.  
17887753 S.Lin, S.G.Van Lanen, and B.Shen (2007).
Regiospecific chlorination of (S)-beta-tyrosyl-S-carrier protein catalyzed by SgcC3 in the biosynthesis of the enediyne antitumor antibiotic C-1027.
  J Am Chem Soc, 129, 12432-12438.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.