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PROSITE documentation PDOC00066

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{PDOC00066}
{PS00068; MDH}
{BEGIN}
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* Malate dehydrogenase active site signature *
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Malate dehydrogenase (EC 1.1.1.37) (MDH)  [1,2] catalyzes  the interconversion
of malate to  oxaloacetate utilizing the NAD/NADH  cofactor system. The enzyme
participates in the citric acid cycle and exists in all aerobics organisms.

While prokaryotic organisms contains a single form of MDH, in eukaryotic cells
there are  two  isozymes: one which is located in the mitochondrial matrix and
the other in the cytoplasm.  Fungi  and  plants also harbor a glyoxysomal form
which  functions in the glyoxylate pathway. In plants chloroplast there is an
additional  NADP-dependent form of  MDH (EC 1.1.1.82)  which  is essential for
both the universal  C3 photosynthesis (Calvin)  cycle and the more specialized
C4 cycle.

As a signature pattern  for  this enzyme we have chosen a region that includes
two residues  involved in the catalytic mechanism [3]:  an aspartic acid which
is involved  in a  proton relay  mechanism,  and  an  arginine which binds the
substrate.

-Consensus pattern: [LIVM]-T-[TRKMN]-L-D-x(2)-R-[STA]-x(3)-[LIVMFY]
                    [D and R are the active site residues]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: MDH  from  archaebacteria  do  not belong to the above family; they are
 evolutionary related to lactate dehydrogenases [4].

-Last update: November 1995 / Text revised.

[ 1] McAlister-Henn L.
     Trends Biochem. Sci. 13:178-181(1988).
[ 2] Gietl C.
     "Malate dehydrogenase isoenzymes: cellular locations and role in the
     flow of metabolites between the cytoplasm and cell organelles."
     Biochim. Biophys. Acta 1100:217-234(1992).
     PubMed=1610875
[ 3] Birktoft J.J., Rhodes G., Banaszak L.J.
     "Refined crystal structure of cytoplasmic malate dehydrogenase at
     2.5-A resolution."
     Biochemistry 28:6065-6081(1989).
     PubMed=2775751
[ 4] Cendrin F., Chroboczek J., Zaccai G., Eisenberg H., Mevarech M.
     "Cloning, sequencing, and expression in Escherichia coli of the gene
     coding for malate dehydrogenase of the extremely halophilic
     archaebacterium Haloarcula marismortui."
     Biochemistry 32:4308-4313(1993).
     PubMed=8476859

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