Identification |
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Name: | Hydroxyacylglutathione hydrolase |
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Synonyms: | |
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Gene Name: | gloB |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in hydrolase activity |
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Specific Function: | Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid |
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Cellular Location: | Cytoplasmic |
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SMPDB Pathways: | Not Available |
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KEGG Pathways: | |
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KEGG Reactions: | | | | | |
1.0S-(2-Hydroxyacyl)glutathione | + | 1.0 | ↔ | 1.0 | + | 1.02-Hydroxy carboxylate |
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SMPDB Reactions: | |
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EcoCyc Reactions: | |
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Complex Reactions: | |
1.0S-(2-hydroxyacyl)glutathione | + | 1.0 | → | 1.0 | + | 1.0a 2-hydroxy carboxylate |
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Metabolites: | |
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GO Classification: | Function |
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binding | catalytic activity | cation binding | hydrolase activity | hydrolase activity, acting on ester bonds | hydroxyacylglutathione hydrolase activity | ion binding | metal ion binding | thiolester hydrolase activity | transition metal ion binding | zinc ion binding |
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Gene Properties |
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Blattner: | b0212 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 5.04 |
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Left Sequence End | 234027 |
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Right Sequence End | 234782 |
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Gene Sequence: | >756 bp
ATGAATCTTAACAGTATTCCCGCCTTTGATGACAATTACATCTGGGTTTTGAATGATGAA
GCAGGTCGCTGCCTGATTGTCGATCCCGGAGACGCAGAGCCAGTATTAAACGCCATTGCC
GCCAATAACTGGCAACCGGAGGCCATATTTCTCACCCACCATCACCACGATCACGTTGGC
GGCGTAAAAGAACTGGTGGAAAAGTTTCCACAAATTGTGGTGTATGGTCCACAAGAGACA
CAAGATAAGGGAACAACACAGGTAGTCAAAGATGGCGAAACTGCCTTCGTTTTGGGGCAT
GAATTTAGTGTAATTGCTACGCCGGGTCACACTTTAGGACATATCTGTTACTTCAGTAAA
CCTTATCTATTTTGCGGCGACACACTGTTTTCTGGTGGGTGTGGTCGGTTGTTTGAAGGG
ACAGCATCACAAATGTATCAATCACTTAAAAAGTTAAGTGCGTTACCTGACGATACATTG
GTATGTTGTGCTCATGAATATACCTTATCAAATATGAAGTTTGCTTTGAGTATTCTTCCG
CACGATTTGTCCATAAATGATTATTATCGTAAAGTTAAGGAGTTACGGGCAAAAAATCAA
ATAACACTACCCGTAATTCTGAAAAATGAGCGGCAAATTAATGTTTTTTTAAGAACGGAA
GATATTGATTTAATTAATGTAATTAATGAAGAAACATTATTGCAACAACCTGAAGAGCGT
TTTGCATGGTTAAGGTCAAAGAAAGATAGGTTCTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 251 |
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Protein Molecular Weight: | 28434 |
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Protein Theoretical pI: | 6 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Hydroxyacylglutathione hydrolase
MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVG
GVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSK
PYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTLVCCAHEYTLSNMKFALSILP
HDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEER
FAWLRSKKDRF |
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References |
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External Links: | |
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General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- O'Young, J., Sukdeo, N., Honek, J. F. (2007). "Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme." Arch Biochem Biophys 459:20-26. Pubmed: 17196158
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