true
1995-11-01
2024-03-27
161
LGUL_SCHPO
The genome sequence of Schizosaccharomyces pombe.
Wood V.
Gwilliam R.
Rajandream M.A.
Lyne M.H.
Lyne R.
Stewart A.
Sgouros J.G.
Peat N.
Hayles J.
Baker S.G.
Basham D.
Bowman S.
Brooks K.
Brown D.
Brown S.
Chillingworth T.
Churcher C.M.
Collins M.
Connor R.
Cronin A.
Davis P.
Feltwell T.
Fraser A.
Gentles S.
Goble A.
Hamlin N.
Harris D.E.
Hidalgo J.
Hodgson G.
Holroyd S.
Hornsby T.
Howarth S.
Huckle E.J.
Hunt S.
Jagels K.
James K.D.
Jones L.
Jones M.
Leather S.
McDonald S.
McLean J.
Mooney P.
Moule S.
Mungall K.L.
Murphy L.D.
Niblett D.
Odell C.
Oliver K.
O'Neil S.
Pearson D.
Quail M.A.
Rabbinowitsch E.
Rutherford K.M.
Rutter S.
Saunders D.
Seeger K.
Sharp S.
Skelton J.
Simmonds M.N.
Squares R.
Squares S.
Stevens K.
Taylor K.
Taylor R.G.
Tivey A.
Walsh S.V.
Warren T.
Whitehead S.
Woodward J.R.
Volckaert G.
Aert R.
Robben J.
Grymonprez B.
Weltjens I.
Vanstreels E.
Rieger M.
Schaefer M.
Mueller-Auer S.
Gabel C.
Fuchs M.
Duesterhoeft A.
Fritzc C.
Holzer E.
Moestl D.
Hilbert H.
Borzym K.
Langer I.
Beck A.
Lehrach H.
Reinhardt R.
Pohl T.M.
Eger P.
Zimmermann W.
Wedler H.
Wambutt R.
Purnelle B.
Goffeau A.
Cadieu E.
Dreano S.
Gloux S.
Lelaure V.
Mottier S.
Galibert F.
Aves S.J.
Xiang Z.
Hunt C.
Moore K.
Hurst S.M.
Lucas M.
Rochet M.
Gaillardin C.
Tallada V.A.
Garzon A.
Thode G.
Daga R.R.
Cruzado L.
Jimenez J.
Sanchez M.
del Rey F.
Benito J.
Dominguez A.
Revuelta J.L.
Moreno S.
Armstrong J.
Forsburg S.L.
Cerutti L.
Lowe T.
McCombie W.R.
Paulsen I.
Potashkin J.
Shpakovski G.V.
Ussery D.
Barrell B.G.
Nurse P.
doi:10.1038/nature724
2002
Nature
415
871-880
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
972 / ATCC 24843
Identification of thermostable glyoxalase I in the fission yeast Schizosaccharomyces pombe.
Takatsume Y.
Izawa S.
Inoue Y.
doi:10.1007/s00203-004-0666-4
2004
Arch. Microbiol.
181
371-377
FUNCTION
CATALYTIC ACTIVITY
COFACTOR
BIOPHYSICOCHEMICAL PROPERTIES
PATHWAY
SUBUNIT
22
glo1
Eukaryota
Pyruvate metabolism
GlxI_Zn
2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1
Glyas_Bleomycin-R_OHBP_Dase
Glyas_Fos-R_dOase_dom
Glyoxalase_1
Glyoxalase_1_CS
VOC
glyox_I
LACTOYLGLUTATHIONE LYASE
LACTOYLGLUTATHIONE LYASE GLYOXALASE I
Glyoxalase
Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
GLYOXALASE_I_1
GLYOXALASE_I_2
VOC
Lactoylglutathione lyase
4.4.1.5
Aldoketomutase
Glyoxalase I
Glx I
Ketone-aldehyde mutase
Methylglyoxalase
S-D-lactoylglutathione methylglyoxal lyase
glo1
SPBC12C2.12c
SPBC21D10.03c
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Binds 1 zinc ion per subunit. Cobalt, nickel and manganese ions can also function as cofactors.
1.6 mM for methylglyoxal (at pH 7.0 and 25 degrees Celsius)
0.8 mM for glutathione (at pH 7.0 and 25 degrees Celsius)
0.24 mM for phenylglyoxal (at pH 7.0 and 25 degrees Celsius)
2 mmol/min/mg enzyme with methylglyoxal as substrate (at pH 7.0 and 25 degrees Celsius)
197 umol/min/mg enzyme with phenylglyoxal as substrate (at pH 7.0 and 25 degrees Celsius)
Optimum pH is 5.5-7.5.
Monomer.
Belongs to the glyoxalase I family.
Lactoylglutathione lyase
34410
1
302
VOC 1
11
153
VOC 2
166
301
Proton donor/acceptor
149
14
18
75
79
99
103
in other chain
in other chain
ligand shared between dimeric partners
substrate
1995-11-01
1
34410
b2368a94f2afd7074cc69b7cd34868ce
MASTTDMSTYKLNHTMIRVKDLDKSLKFYTEVFGMKLIDQWVFEENEFSLSFLAFDGPGALNHGVERSKREGILELTYNFGTEKKEGPVYINGNTEPKRGFGHICFTVDNIESACAYLESKGVSFKKKLSDGKMKHIAFALDPDNYWIELVSQSETKPKANISNFRFNHTMVRVKDPEPSIAFYEKLGMKVIDKADHPNGKFTNYFLAYPSDLPRHDREGLLELTHNWGTEKESGPVYHNGNDGDEKGYGHVCISVDNINAACSKFEAEGLPFKKKLTDGRMKDIAFLLDPDNYWVEVIEQK
true
true
true
true
true
true
true
true
true
true
true