PMID- 10404729
OWN - NLM
STAT- MEDLINE
DCOM- 19990824
LR  - 20190706
IS  - 0009-8981 (Print)
IS  - 0009-8981 (Linking)
VI  - 283
IP  - 1-2
DP  - 1999 May
TI  - Three point mutations of human butyrylcholinesterase in a Japanese family and the
      alterations of three-dimensional structure.
PG  - 33-42
AB  - Three different mutations at codons 330 (TTA to ATA), 365 (GGA to AGA) and 515
      (CGT to TGT) of human butyrylcholinesterase (hBChE) were identified in a Japanese
      family. We correlated alterations in in the patient's hBChE activity with
      possible structural alterations in the three-dimensional structure of hBChE
      caused by the point mutations. This study was performed using the published
      computer-generated three-dimensional structure of hBChE based on the structure of
      acetylcholinesterase. The amino acid substitution at L330I was adjacent to
      hydrophobic residues that form the channel domain of the active center. This side
      chain faced the side opposite the active center. The amino acid substitution at
      G365R was located at the position most remote from the active center, and this
      substitution site was exposed to the surface of the BChE protein. Alpha-helical
      structure was present to the active center, and the guanidyl residue of native
      Arg 515 was hydrogen-bonded to the carboxyl group of Asp 395 in the alpha-helix. 
      These point mutations may cause steric effects on the present patient's hBChE
      activity. This is the first report of three-dimensional structural analysis
      performed on the L330I, G365R, and R515C mutations of hBChE.
FAU - Asanuma, K
AU  - Asanuma K
AD  - Department of Laboratory Diagnosis, Sapporo Medical University School of
      Medicine, Japan.
FAU - Yagihashi, A
AU  - Yagihashi A
FAU - Uehara, N
AU  - Uehara N
FAU - Kida, T
AU  - Kida T
FAU - Watanabe, N
AU  - Watanabe N
LA  - eng
PT  - Case Reports
PT  - Journal Article
PL  - Netherlands
TA  - Clin Chim Acta
JT  - Clinica chimica acta; international journal of clinical chemistry
JID - 1302422
RN  - EC 3.1.1.8 (Butyrylcholinesterase)
SB  - IM
MH  - Adult
MH  - Butyrylcholinesterase/*chemistry/deficiency/*genetics
MH  - Computer Simulation
MH  - Female
MH  - Humans
MH  - Japan
MH  - Male
MH  - Models, Molecular
MH  - Pedigree
MH  - *Point Mutation
MH  - Polymerase Chain Reaction
MH  - Polymorphism, Restriction Fragment Length
MH  - Protein Conformation
MH  - Sequence Analysis, DNA
EDAT- 1999/07/15 00:00
MHDA- 1999/07/15 00:01
CRDT- 1999/07/15 00:00
PHST- 1999/07/15 00:00 [pubmed]
PHST- 1999/07/15 00:01 [medline]
PHST- 1999/07/15 00:00 [entrez]
AID - S0009-8981(99)00030-3 [pii]
AID - 10.1016/s0009-8981(99)00030-3 [doi]
PST - ppublish
SO  - Clin Chim Acta. 1999 May;283(1-2):33-42. doi: 10.1016/s0009-8981(99)00030-3.