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InterPro: IPR018177 L-lactate dehydrogenase, active site

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UniProtKB

Matches:

1447 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
Matches in BioMart

Accession

IPR018177 L-lactate_DH_AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00064	L_LDH	1447
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001236 Lactate/malate dehydrogenase
IPR001557 L-lactate/malate dehydrogenase
IPR011304 L-lactate dehydrogenase
IPR015955 Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0004459 L-lactate dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents the NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes. This enzyme functions as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified [1] which can discriminate between the two activities.

This entry represents an active site of the L-lactate dehydrogenase enzyme, and includes a conserved histidine which is essential to the catalytic mechanism.

Structural links Help

PDB - click here

SCOP: d.162.1.1 , i.12.1.1

CATH: 3.90.110.10

Database links Help

Enzyme: EC:1.1.1.27

CluSTr: ALLvsALL:2334:60.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018177

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00338 L-lactate dehydrogenase A chain

P00342 L-lactate dehydrogenase C chain

P00343 L-lactate dehydrogenase

Q27888 L-lactate dehydrogenase

Q95028 L-lactate dehydrogenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001236	Lactate/malate dehydrogenase
IPR016040	NAD(P)-binding domain
IPR011304	L-lactate dehydrogenase
IPR018177	L-lactate dehydrogenase, active site
IPR001557	L-lactate/malate dehydrogenase
IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Hannenhalli SS, Russell RB. Analysis and prediction of functional sub-types from protein sequence alignments. J. Mol. Biol. 303 61-76 2000 [PubMed: 11021970] http://dx.doi.org/10.1006/jmbi.2000.4036

Additional Reading Open in usermanual
	Lee BI, Chang C, Cho SJ, Eom SH, Kim KK, Yu YG, Suh SW. Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. J. Mol. Biol. 307 2001 1351-62 [PubMed: 11292347] http://dx.doi.org/10.1006/jmbi.2001.4532
	Hendriks W, Mulders JW, Bibby MA, Slingsby C, Bloemendal H, de Jong WW. Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions. Proc. Natl. Acad. Sci. U.S.A. 85 1988 7114-8 [PubMed: 3174623] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=3174623
	Uchikoba H, Fushinobu S, Wakagi T, Konno M, Taguchi H, Matsuzawa H. Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces. Proteins 46 2002 206-14 [PubMed: 11807949] http://dx.doi.org/10.1002/prot.1165
	Coquelle N, Fioravanti E, Weik M, Vellieux F, Madern D. Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments. J. Mol. Biol. 374 2007 547-62 [PubMed: 17936781] http://dx.doi.org/10.1016/j.jmb.2007.09.049
	Cameron A, Read J, Tranter R, Winter VJ, Sessions RB, Brady RL, Vivas L, Easton A, Kendrick H, Croft SL, Barros D, Lavandera JL, Martin JJ, Risco F, Garcia-Ochoa S, Gamo FJ, Sanz L, Leon L, Ruiz JR, Gabarro R, Mallo A, Gomez de las Heras F. Identification and activity of a series of azole-based compounds with lactate dehydrogenase-directed anti-malarial activity. J. Biol. Chem. 279 2004 31429-39 [PubMed: 15117937] http://dx.doi.org/10.1074/jbc.M402433200
	Irimia A, Vellieux FM, Madern D, Zaccai G, Karshikoff A, Tibbelin G, Ladenstein R, Lien T, Birkeland NK. The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation. J. Mol. Biol. 335 2004 343-56 [PubMed: 14659762] http://dx.doi.org/10.1016/j.jmb.2003.10.054
	Lerch HP, Frank R, Collins J. Cloning, sequencing and expression of the L-2-hydroxyisocaproate dehydrogenase-encoding gene of Lactobacillus confusus in Escherichia coli. Gene 83 1989 263-70 [PubMed: 2684788] http://dx.doi.org/10.1016/0378-1119(89)90112-1

InterPro 23.1