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Human Metabolome Database Version 2.5

 

Showing metabocard for D-Lactaldehyde (HMDB06458)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-05-23 10:54:11
Update Date 2009-05-05 21:00:50
Accession Number HMDB06458
Secondary Accession Numbers HMDB06949
Common Name D-Lactaldehyde
Description D- and L-lactaldehyde are also good substrates for aldose reductase. The aldose reductase-catalyzed reduction of methylglyoxal produces 95% acetol, 5% D-lactaldehyde. (PMID: 1537826) D-lactaldehyde is an intermediate in the pyruvate metabolic pathway. Pyruvaldehyde is irreversibly produced from D-lactaldehyde via the enzyme glyoxylate reductase (NADP+, Swiss-Prot: Q5T945).
Synonyms
  1. (2R)-2-hydroxypropanal
  2. (R)-Lactaldehyde
  3. D-2-hydroxypropionaldehyde
  4. D-lactaldehyde
Chemical IUPAC Name (2R)-2-hydroxypropanal
Chemical Formula C3H6O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Ketones and aldehydes
Class
  • Aldehydes
  • Alcohols and Polyols
Sub Class
  • Short chain aldehydes
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • secondary alcohol
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 74.078
Monoisotopic Molecular Weight 74.036781
Isomeric SMILES C[C@@H](O)C=O
Canonical SMILES CC(O)C=O
KEGG Compound ID C00937 Link Image
BioCyc ID CPD-358 Link Image
BiGG ID 36414 Link Image
Wikipedia Link Lactaldehyde Link Image
NuGOwiki Link HMDB06458 Link Image
Metagene Link HMDB06458 Link Image
METLIN ID Not Available
PubChem Compound 439350 Link Image
PubChem Substance 10298304 Link Image
ChEBI ID 17167 Link Image
CAS Registry Number 3946-09-6
InChI Identifier InChI=1/C3H6O2/c1-3(5)2-4/h2-3,5H,1H3/t3-/m1/s1
Synthesis Reference Lobell, Mario, Grout, David H. G. New insight into the pyruvate decarboxylase-catalyzed formation of lactaldehyde from H-D exchange experiments: a 'water proof' active site. Journal of the Chemical Society, Perkin Transactions 1: Organic and Bio-Organic Chemistry (1996), (13), 1577-1581; Kranz, Cyrill. Synthesis of Lactic Aldehyde. Chemicke Listy pro Vedu a Prumysl (1912), 5 323-7.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 658.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.2 [Predicted by PubChem via XLOGP]; -1.04 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Mitochondria
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Pyruvate Metabolism SMP00060 Link Image map00620 Link Image
General References
  1. Vander Jagt DL, Robinson B, Taylor KK, Hunsaker LA: Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. J Biol Chem. 1992 Mar 5;267(7):4364-9. [PubMed Link Image]
  2. Hazen SL, Hsu FF, d'Avignon A, Heinecke JW: Human neutrophils employ myeloperoxidase to convert alpha-amino acids to a battery of reactive aldehydes: a pathway for aldehyde generation at sites of inflammation. Biochemistry. 1998 May 12;37(19):6864-73. [PubMed Link Image]
  3. HUANG PC, MILLER ON: The metabolism of lactaldehyde. V. Metabolism of L-fucose. J Biol Chem. 1958 Mar;231(1):201-5. [PubMed Link Image]
  4. Wikipedia Link Image
Metabolic Enzymes
  1. Aldose reductase
  2. Glyoxylate reductase/hydroxypyruvate reductase
Enzyme 1 [top]
Enzyme 1 ID 5320
Enzyme 1 Name Aldose reductase
Enzyme 1 Synonyms
  1. AR
  2. Aldehyde reductase
Enzyme 1 Gene Name AKR1B1
Enzyme 1 Protein Sequence >Aldose reductase 
MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQ
EKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK
EFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKP
AVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAK
HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCA
LLSCTSHKDYPFHEEF
Enzyme 1 Number of Residues 316
Enzyme 1 Molecular Weight 35854
Enzyme 1 Theoretical pI 6.99
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
—
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies
Enzyme 1 Pathways
Enzyme 1 Reactions
  • alditol + NAD(P)+ = aldose + NAD(P)H + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 178487 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P15121 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ALDR_HUMAN Link Image
Enzyme 1 PDB ID 1T40 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >951 bp 
ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC
TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC
CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG
GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG
TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG
AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG
GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC
ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC
AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT
GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC
CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG
GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG
CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG
ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA
CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC
TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA
Enzyme 1 GenBank Gene ID J04795 Link Image
Enzyme 1 GeneCard ID AKR1B1 Link Image
Enzyme 1 GenAtlas ID AKR1B1 Link Image
Enzyme 1 HGNC ID HGNC:381 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed Link Image]
  2. Chung S, LaMendola J: Cloning and sequence determination of human placental aldose reductase gene. J Biol Chem. 1989 Sep 5;264(25):14775-7. [PubMed Link Image]
  3. Graham A, Hedge PJ, Powell SJ, Riley J, Brown L, Gammack A, Carey F, Markham AF: Nucleotide sequence of cDNA for human aldose reductase. Nucleic Acids Res. 1989 Oct 25;17(20):8368. [PubMed Link Image]
  4. Grundmann U, Bohn H, Obermeier R, Amann E: Cloning and prokaryotic expression of a biologically active human placental aldose reductase. DNA Cell Biol. 1990 Apr;9(3):149-57. [PubMed Link Image]
  5. Nishimura C, Matsuura Y, Kokai Y, Akera T, Carper D, Morjana N, Lyons C, Flynn TG: Cloning and expression of human aldose reductase. J Biol Chem. 1990 Jun 15;265(17):9788-92. [PubMed Link Image]
  6. Graham A, Brown L, Hedge PJ, Gammack AJ, Markham AF: Structure of the human aldose reductase gene. J Biol Chem. 1991 Apr 15;266(11):6872-7. [PubMed Link Image]
  7. Ko BC, Ruepp B, Bohren KM, Gabbay KH, Chung SS: Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J Biol Chem. 1997 Jun 27;272(26):16431-7. [PubMed Link Image]
  8. Ferraretto A, Negri A, Giuliani A, De Grada L, Fuhrman Conti AM, Ronchi S: Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. Biochim Biophys Acta. 1993 Feb 17;1175(3):283-8. [PubMed Link Image]
  9. Morjana NA, Lyons C, Flynn TG: Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem. 1989 Feb 15;264(5):2912-9. [PubMed Link Image]
  10. Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK: Identification of the reactive cysteine residue in human placenta aldose reductase. Biochim Biophys Acta. 1993 Aug 7;1164(3):268-72. [PubMed Link Image]
  11. Jaquinod M, Potier N, Klarskov K, Reymann JM, Sorokine O, Kieffer S, Barth P, Andriantomanga V, Biellmann JF, Van Dorsselaer A: Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. Eur J Biochem. 1993 Dec 15;218(3):893-903. [PubMed Link Image]
  12. Tarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM: Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem. 1993 Dec 5;268(34):25687-93. [PubMed Link Image]
  13. Wilson DK, Bohren KM, Gabbay KH, Quiocho FA: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science. 1992 Jul 3;257(5066):81-4. [PubMed Link Image]
  14. Borhani DW, Harter TM, Petrash JM: The crystal structure of the aldose reductase.NADPH binary complex. J Biol Chem. 1992 Dec 5;267(34):24841-7. [PubMed Link Image]
  15. Wilson DK, Tarle I, Petrash JM, Quiocho FA: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):9847-51. [PubMed Link Image]
  16. Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH: The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry. 1997 Dec 23;36(51):16134-40. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13057
Enzyme 2 Name Glyoxylate reductase/hydroxypyruvate reductase
Enzyme 2 Synonyms
  1. Glyoxylate reductase/hydroxypyruvate reductase, isoform CRA_b
Enzyme 2 Gene Name GRHPR
Enzyme 2 Protein Sequence >Glyoxylate reductase/hydroxypyruvate reductase 
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLS
DHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLL
TTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRF
LYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVF
INISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHR
TRNTMSLLAANNLLAGLRGEPMPSELKL
Enzyme 2 Number of Residues 328
Enzyme 2 Molecular Weight 35669
Enzyme 2 Theoretical pI 7.44
Enzyme 2 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • L-serine biosynthesis
  • L-serine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID Q5T945 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q5T945_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AL158155 Link Image
Enzyme 2 GeneCard ID Q5T945 Link Image
Enzyme 2 GenAtlas ID GRHPR Link Image
Enzyme 2 HGNC ID HGNC:4570 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available