MG_172_MONOMER – methionine aminopeptidase, type I

Name
WID MG_172_MONOMER View in model
Name methionine aminopeptidase, type I View in model
Cross references PDB: 1MAT, PDB: 4MAT
 
Genetics
Gene MG_172 View in model
 
Structure
Sequence
1
51
101
151
201
MIYLKSANEVAGIKKACAIFKAVKAYFTIEKLLGKKLVTIDRLIKQFIEQ
KQAKCAFHGYLGFPGFNCLSLNQTVIHGVADQTVFKDSDKLTLDIGIDYH
GYLCDAAFTLLGNKADPKAVKLLNDVEQAFSKVIEPELFVNNPIGNLSNA
IQTYFENKGYFLVKEFGGHGCGIKIHEDPLILNWGEKNQGVRLQEGMVIC
IEPMVMTDSSEITMAANNWNVLTLKSKFNCHVEQMYHITNNGFECLTN*
50
100
150
200
249
 View in model
Is N‑terminal methionine cleaved
No
 View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H1959C1256N322O358S14
Molecular weight (pH 7.5; Da) 27746.77 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)		 23920
Instability index 29.88
Is stable True
Aliphatic index 94.38
GRAVY (25C, pH 7.0) -0.0217
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)		 1200 View in model
 
Synthesis
Localization c View in model
 
Function
Enzyme N-terminal methionine cleavage
[c]: H2O + MetMet ⇒ (2) MET		 View in model
 
Parameters
Parameters Parameter_0103: methionineAminoPeptidaseSpecificRate = 6 1/s View in model
 
Comments
Comments Functional Macromolecule Functional as monomer [PUB_0025]. Coenzymes Interacts with 2 CO or FE2 per monomer as prosthetic group [24,96].
References

  1. Kendall RL, Bradshaw RA. Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins. J Biol Chem 267, 20667-73 (1992). WholeCell: PUB_0025, PubMed: 1328207
 
Metadata
Created 2012-10-01 15:07:51
Last updated 2012-10-01 15:14:31