PMID- 10075721
OWN - NLM
STAT- MEDLINE
DCOM- 19990415
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 12
DP  - 1999 Mar 19
TI  - Cloning and characterization of human guanine deaminase. Purification and partial
      amino acid sequence of the mouse protein.
PG  - 8175-80
AB  - Mouse erythrocyte guanine deaminase has been purified to homogeneity. The native 
      enzyme was dimeric, being comprised of two identical subunits of approximately
      50,000 Da. The protein sequence was obtained from five cyanogen bromide cleavage 
      products giving sequences ranging from 12 to 25 amino acids in length and
      corresponding to 99 residues. Basic Local Alignment Search Tool (BLAST) analysis 
      of expressed sequence databases enabled the retrieval of a human expressed
      sequence tag cDNA clone highly homologous to one of the mouse peptide sequences. 
      The presumed coding region of this clone was used to screen a human kidney cDNA
      library and secondarily to polymerase chain reaction-amplify the full-length
      coding sequence of the human brain cDNA corresponding to an open reading frame of
      1365 nucleotides and encoding a protein of 51,040 Da. Comparison of the mouse
      peptide sequences with the inferred human protein sequence revealed 88 of 99
      residues to be identical. The human coding sequence of the putative enzyme was
      subcloned into the bacterial expression vector pMAL-c2, expressed, purified, and 
      characterized as having guanine deaminase activity with a Km for guanine of 9.5
      +/- 1.7 microM. The protein shares a 9-residue motif with other aminohydrolases
      and amidohydrolases (PGX[VI]DXH[TVI]H) that has been shown to be ligated with
      heavy metal ions, commonly zinc. The purified recombinant guanine deaminase was
      found to contain approximately 1 atom of zinc per 51-kDa monomer.
FAU - Yuan, G
AU  - Yuan G
AD  - Department of Medical Genetics, Faculty of Medicine, University of Calgary,
      Calgary, Alberta T2N 4N1, Canada.
FAU - Bin, J C
AU  - Bin JC
FAU - McKay, D J
AU  - McKay DJ
FAU - Snyder, F F
AU  - Snyder FF
LA  - eng
SI  - GENBANK/AF095286
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 3.5.4.3 (Guanine Deaminase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Brain/enzymology
MH  - Catalysis
MH  - Cloning, Molecular
MH  - Guanine Deaminase/*genetics
MH  - Humans
MH  - Kidney/enzymology
MH  - Kinetics
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Molecular Sequence Data
MH  - Molecular Weight
EDAT- 1999/03/13 00:00
MHDA- 1999/03/13 00:01
CRDT- 1999/03/13 00:00
PHST- 1999/03/13 00:00 [pubmed]
PHST- 1999/03/13 00:01 [medline]
PHST- 1999/03/13 00:00 [entrez]
AID - 10.1074/jbc.274.12.8175 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 19;274(12):8175-80. doi: 10.1074/jbc.274.12.8175.