spacer
spacer

PDBsum entry 4flc

Go to PDB code: 
protein Protein-protein interface(s) links
Lyase PDB id
4flc
Jmol
Contents
Protein chain
460 a.a.
Waters ×144
PDB id:
4flc
Name: Lyase
Title: Structural and biochemical characterization of human adenylo lyase (adsl) and the r303c adsl deficiency associated mutat
Structure: Adenylosuccinate lyase. Chain: a, b, c, d. Synonym: asl, adenylosuccinase, asase. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: adsl, amps. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.60Å     R-factor:   0.234     R-free:   0.298
Authors: M.K.Deaton,S.P.Ray,G.C.Capodagli,L.A.F.Calkins,L.Sawle,K.Gho D.Patterson,S.D.Pegan
Key ref: S.P.Ray et al. (2012). Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation. Biochemistry, 51, 6701-6713. PubMed id: 22812634
Date:
14-Jun-12     Release date:   01-Aug-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P30566  (PUR8_HUMAN) -  Adenylosuccinate lyase
Seq:
Struc:
484 a.a.
460 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.4.3.2.2  - Adenylosuccinate lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Purine Biosynthesis (late stages)
      Reaction:
1. N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP
2. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide
N(6)-(1,2-dicarboxyethyl)AMP
= fumarate
+ AMP
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate
= fumarate
+ 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   2 terms 
  Biological process     'de novo' AMP biosynthetic process   17 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    reference    
 
 
Biochemistry 51:6701-6713 (2012)
PubMed id: 22812634  
 
 
Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation.
S.P.Ray, M.K.Deaton, G.C.Capodagli, L.A.Calkins, L.Sawle, K.Ghosh, D.Patterson, S.D.Pegan.
 
  ABSTRACT  
 
No abstract given.