BMRB: 2229

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: 2.3 %, Completeness: 1.0 %, Completeness (bb): 1.6 % Detail

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Polymer type: polypeptide(L)

	Total	13C
All	1.0 % (14 of 1403)	1.0 % (14 of 1403)
Backbone	1.6 % (15 of 915)	1.6 % (15 of 915)
Sidechain	0.9 % (7 of 783)	0.9 % (7 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

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Sample

Temperature 283 K, pH 6.4

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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: , Abstract

Related entities 1. aspartate transcarbamoylase, : 1 : 9 : 42 : 1 : 193 entities Detail

Interaction partners 1. aspartate transcarbamoylase, : 4 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail