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The Role of an Active Site Histidine in the Catalytic Mechanism of Aspartate Transcarbamoylase
Authors
Kleanthous, C., Wemmer, D., Schachman, H.K.
Assembly
aspartate transcarbamoylase
Entity
1. aspartate transcarbamoylase (polymer), 310 monomers, 34295.74 Da Detail

ANPLYQKHII SINDLSRDDL NLVLATAAKL KANPQPELLK HKVIASCFFE ASTRTRLSFQ TSMHRLGASV VGFSDSANTS LGKKGETLAD TISVISTYVD AIVMRHPQEG AARLATEFSG NVPVLNAGDG SNQHPTQTLL DLFTIQQTEG RLDNLHVAMV GDLKYGRTVH SLTQALAKFD GNRFYFIAPD ALAMPEYILD MLDEKGIAWS LHSSIEEVMA EVDILYMTRV QKERLDPSEY ANVKAQFVLR ASDLHNAKAN MKVLHPLPRV DEIATDVDKT PHAWYFQQAG NGIFARQALL ALVLNRDLVL


Formula weight
34295.74 Da
Source organism
Escherichia coli
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 1.6 %, Completeness: 0.9 %, Completeness (bb): 1.1 % Detail

Polymer type: polypeptide(L)

Total13C
All 0.9 % (13 of 1403) 0.9 % (13 of 1403)
Backbone 1.1 % (10 of 915) 1.1 % (10 of 915)
Sidechain 0.8 % (6 of 783) 0.8 % (6 of 783)
Aromatic 0.0 % (0 of 124) 0.0 % (0 of 124)
Methyl 0.0 % (0 of 202) 0.0 % (0 of 202)

1. aspartate transcarbamoylase

ANPLYQKHII SINDLSRDDL NLVLATAAKL KANPQPELLK HKVIASCFFE ASTRTRLSFQ TSMHRLGASV VGFSDSANTS LGKKGETLAD TISVISTYVD AIVMRHPQEG AARLATEFSG NVPVLNAGDG SNQHPTQTLL DLFTIQQTEG RLDNLHVAMV GDLKYGRTVH SLTQALAKFD GNRFYFIAPD ALAMPEYILD MLDEKGIAWS LHSSIEEVMA EVDILYMTRV QKERLDPSEY ANVKAQFVLR ASDLHNAKAN MKVLHPLPRV DEIATDVDKT PHAWYFQQAG NGIFARQALL ALVLNRDLVL

Sample

Temperature 283 K, pH 6.4



Release date
1995-07-30
Citation
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase
Kleanthous, C., Wemmer, D., Schachman, H.K.
J. Biol. Chem. (1988), 263, 13062-13067, PubMed 3047117 , DOI: ,
Related entities 1. aspartate transcarbamoylase, : 1 : 9 : 40 : 1 : 148 entities Detail
Interaction partners 1. aspartate transcarbamoylase, : 4 interactors Detail
Experiments performed 1 experiments Detail