Hmdb loader
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP00812
Secondary Accession Numbers
  • 6092
  • HMDBP05975
Name Hydroxyacylglutathione hydrolase, mitochondrial
Synonyms
  1. Glx II
  2. Glyoxalase II
Gene Name HAGH
Protein Type Unknown
Biological Properties
General Function Involved in hydrolase activity
Specific Function Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Pathways
  • Leigh Syndrome
  • methylglyoxal degradation
  • Primary hyperoxaluria II, PH2
  • Pyruvaldehyde Degradation
  • Pyruvate Decarboxylase E1 Component Deficiency (PDHE1 Deficiency)
  • Pyruvate Dehydrogenase Complex Deficiency
  • Pyruvate kinase deficiency
  • Pyruvate metabolism
  • Pyruvate metabolism
Reactions
S-(2-hydroxyacyl)glutathione + Water → Glutathione + a 2-hydroxy carboxylate details
S-Lactoylglutathione + Water → Glutathione + D-Lactic acid details
GO Classification
Biological Process
glutathione biosynthetic process
carbohydrate metabolic process
Cellular Component
mitochondrial matrix
cytoplasm
Function
ion binding
cation binding
metal ion binding
hydrolase activity, acting on ester bonds
binding
catalytic activity
hydrolase activity
transition metal ion binding
zinc ion binding
hydroxyacylglutathione hydrolase activity
thiolester hydrolase activity
Molecular Function
metal ion binding
zinc ion binding
hydroxyacylglutathione hydrolase activity
Cellular Location
  1. Isoform 2:Cytoplasm
Gene Properties
Chromosome Location 16
Locus 16p13.3
SNPs HAGH
Gene Sequence
>927 bp
ATGGTGGTGGGCCGAGGGCTGCTCGGCCGCCGCAGCCTCGCCGCGCTGGGAGCCGCCTGC
GCCCGCCGAGGCCTCGGTCCAGCCCTGCTGGGAGTTTTCTGCCACACAGATTTGCGGAAG
AACCTGACCGTGGACGAGGGCACCATGAAGGTAGAGGTGCTGCCTGCCCTGACCGACAAC
TACATGTACCTGGTCATTGATGATGAGACCAAGGAGGCTGCCATTGTGGATCCGGTGCAG
CCCCAGAAGGTCGTGGACGCGGCGAGAAAGCACGGGGTGAAACTGACCACAGTGCTCACC
ACCCACCACCACTGGGACCATGCTGGCGGGAATGAGAAACTGGTCAAGCTGGAGTCGGGA
CTGAAGGTGTACGGGGGTGACGACCGTATCGGGGCCCTGACTCACAAGATCACTCACCTG
TCCACACTGCAGGTGGGGTCTCTGAACGTCAAGTGCCTGGCGACCCCGTGCCACACTTCA
GGACACATTTGTTACTTCGTGAGCAAGCCCGGAGGCTCGGAGCCCCCTGCCGTGTTCACA
GGTGACACCTTGTTTGTGGCTGGCTGCGGGAAGTTCTATGAAGGGACTGCGGATGAGATG
TGTAAAGCTCTGCTGGAGGTCTTGGGCCGGCTCCCCCCGGACACAAGAGTCTACTGTGGC
CACGAGTACACCATCAACAACCTCAAGTTTGCACGCCACGTGGAGCCCGGCAATGCCGCC
ATCCGGGAGAAGCTGGCCTGGGCCAAGGAGAAGTACAGCATCGGGGAGCCCACAGTGCCA
TCCACCCTGGCAGAGGAGTTTACCTACAACCCCTTCATGAGAGTGAGGGAGAAGACGGTG
CAGCAGCACGCAGGTGAGACGGACCCGGTGACCACCATGCGGGCCGTGCGCAGGGAGAAG
GACCAGTTCAAGATGCCCCGGGACTGA
Protein Properties
Number of Residues 308
Molecular Weight 28859.855
Theoretical pI 7.323
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Hydroxyacylglutathione hydrolase, mitochondrial
MVVGRGLLGRRSLAALGAACARRGLGPALLGVFCHTDLRKNLTVDEGTMKVEVLPALTDN
YMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESG
LKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFT
GDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAA
IREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREK
DQFKMPRD
GenBank ID Protein 94538322
UniProtKB/Swiss-Prot ID Q16775
UniProtKB/Swiss-Prot Entry Name GLO2_HUMAN
PDB IDs
GenBank Gene ID NM_005326.4
GeneCard ID HAGH
GenAtlas ID HAGH
HGNC ID HGNC:4805
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed:15616553 ]
  5. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed:11157797 ]
  6. Ridderstrom M, Saccucci F, Hellman U, Bergman T, Principato G, Mannervik B: Molecular cloning, heterologous expression, and characterization of human glyoxalase II. J Biol Chem. 1996 Jan 5;271(1):319-23. [PubMed:8550579 ]
  7. Cordell PA, Futers TS, Grant PJ, Pease RJ: The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II. J Biol Chem. 2004 Jul 2;279(27):28653-61. Epub 2004 Apr 26. [PubMed:15117945 ]
  8. Cameron AD, Ridderstrom M, Olin B, Mannervik B: Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure. 1999 Sep 15;7(9):1067-78. [PubMed:10508780 ]