Sequence of TTUC_PSEPU
EC Number:4.1.1.73
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(R,R)-tartrate = D-glycerate + CO2
Other sequences found for EC No. 4.1.1.73
General information:
Sequence
0 MPAHSFRIAA IPGDGIGLEV LPEGIRVLEA AALKHGLALE FDTFEWASCD YYLQHGKMMP
60 DDWAEQLKQY DAIYFGAVDW PDKVPDHISL WGSLLKFRRE FDQYVNIRPV RLFPGVPCAL
120 ANRKVGDIDF VVVRENTEGE YSSLGGIMFE NTENEIVIQE SIFTRRGVDR ILKYAFDLAE
180 KRERKHVTSA TKSNGMAISM PYWDKRTEAM AAHYPHVSWD KQHIDILCAR FVLQPERFDV
240 VVVASNLFGD ILSDLGPACA GTIGIAPSAN LNPERNFPSL FEPVHGSAPD IFGKNIANPI
300 AMIWSGALML EFLGQGDERY QRAHDDMLNA IERVIADGSV TPDMGGTLST QQVGAAISDT
360 LARLD
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
878816
Tipton P.A.,Beecher B.S.
Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases.
Arch. Biochem. Biophys.
313
15-21
1994
878817
Tipton P.A.,Peisach J.
Characterization of the multiple catalytic activities of tartrate dehydrogenase.
Biochemistry
29
1749-1756
1990
878818
Tipton P.A.
Intermediate partitioning in the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate.
Biochemistry
32
2822-2827
1993
878819
Karsten W.E.,Tipton P.A.,Cook P.F.
Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD.
Biochemistry
41
12193-12199
2002
