Information on EC 5.3.1.8 - Mannose-6-phosphate isomerase:
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EC NUMBERCOMMENTARY
5.3.1.8-

RECOMMENDED NAMEGeneOntology No.
Mannose-6-phosphate isomeraseGO:0004476

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram		----
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram		analysis of enzyme-substrate and enzyme-inhibitor complexes by ESI-FTICR mass spectrometryEscherichia coli-660706
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram		cis-enediol mechanismPyrobaculum aerophilumQ8ZWV0661100
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram		mechanism does not involve trans-enediol. Instead, activity may result from additional space in the active site which permits rotation of the C2-C3 bondPyrobaculum aerophilumQ8ZWV0662267
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram		hydride transfer mechanism of a alpha-hydrogen bond between the C1 and C2 positions of substrate. Mechanism involves Zn2+ mediating the movement of a proton between O1 and O2, and the hydrophobic environment formed in part by T278 promoting transfer of a hydride ionHomo sapiens-681498
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram		reaction mechanism, overview. Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site. Isomerization probably follows a cis-enediol mechanism, overall folding pattern of the central catalytic domain, overviewSalmonella enterica subsp. enterica serovar TyphimuriumP25081701472

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
aldose-ketose-isomerizationThermus thermophilusQ5SIM4-714372
intramolecular oxidoreduction----
isomerization----

PATHWAYKEGG LinkMetaCyc Link
ascorbate biosynthesis I (L-galactose pathway)-PWY-882
D-mannose degradation-MANNCAT-PWY
GDP-mannose biosynthesis-PWY-5659
mannitol biosynthesis-PWY-3881
mannitol degradation II-PWY-3861

SYSTEMATIC NAMEIUBMB Comments
D-mannose-6-phosphate aldose-ketose-isomeraseA zinc protein.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
BceAJBurkholderia cenocepacia--690577
becABurkholderia cepaciaQ06XM8-671785
D-mannose-6-phosphate ketol-isomerase----
GTMpiGeobacillus thermodenitrificans--702817
Isomerase, mannose phosphate----
ManAPhotorhabdus luminescens--713855
Mannose phosphate isomerase----
mannose-6-phosphate isomeraseThermus thermophilusQ5SIM4-714372
MPIMus musculus--662458
MPISalmonella enterica subsp. enterica serovar TyphimuriumP25081-701472
MPIGeobacillus thermodenitrificans--701812
MPIThermus thermophilus--713854, 714372
PHMSulfolobus solfataricus--680450
Phosphohexoisomerase----
Phosphohexomutase----
PhosphohexomutaseSulfolobus solfataricus--680450
Phosphomannoisomerase----
Phosphomannose isomerase----
Phosphomannose isomerasePyrococcus furiosus-type II phosphomannose isomerase, bifunctional phosphomannose isomerase/GDP-mannose pyrophosphorylase (manC), with both PMI (E.C. 5.3.1.8) and GMP (E.C.2.7.7.13) activities694521
Phosphomannose isomeraseArabidopsis thalianaQ9M884-700488
Phosphomannose isomeraseAlcaligenes sp.--701879
Phosphomannose isomeraseEscherichia coli, Saccharomyces cerevisiae--702663
Phosphomannose isomeraseSphingobium chungbukense--702869
Phosphomannose isomerasePlacopecten magellanicus--705394
Phosphomannose isomeraseAspergillus fumigatusQ66WM4-705568
Phosphomannose isomerasePhotorhabdus luminescens--713855
phosphomannose-isomeraseBrassica napus--706204
phosphomannose-isomeraseOncidium Gower Ramsey--716507
Phosphphexomutase----
PMI----
PMILeishmania mexicanaQ9GRS9-652215
PMIAlcaligenes sp.--701879
PMISphingobium chungbukense--702869
PMIBrassica napus--706204
PMIPhotorhabdus luminescens--713855
PMIOncidium Gower Ramsey--716507
PMI/GMPSphingobium chungbukense--702869
Pmi1Aspergillus fumigatusQ66WM4-705568
PslBPseudomonas aeruginosa--692361
type I phosphomannose isomeraseEscherichia coli--716883
type I phosphomannose isomerasesHomo sapiens--716883
type I PMIEscherichia coli, Homo sapiens--716883

CAS REGISTRY NUMBERCOMMENTARY
9023-88-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Aeropyrum pernixbiunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.662220Q9YE01SwissprotManually annotated by BRENDA team
Alcaligenes sp.strain CGMCC2428701879--Manually annotated by BRENDA team
Alcaligenes sp. CGMCC2428strain CGMCC2428701879--Manually annotated by BRENDA team
Amorphophallus konjac-2809, 2810--Manually annotated by BRENDA team
Apis mellifera-2624--Manually annotated by BRENDA team
Arabidopsis thalianaisoform Pmi1; isoform Pmi2693149--Manually annotated by BRENDA team
Arabidopsis thalianasyncytia induced by nematode Heterodera schachtii700488Q9M884UniProtManually annotated by BRENDA team
Ascaris suum-2624--Manually annotated by BRENDA team
Aspergillus fumigatusstrain YJ-407, gene pmi1705568Q66WM4UniProtManually annotated by BRENDA team
Aspergillus fumigatus YJ-407strain YJ-407, gene pmi1705568Q66WM4UniProtManually annotated by BRENDA team
Bacillus subtilisenzyme from Bacillus subtilis strain HB002; ATCC 23857701797Q9AGZ4UniProtManually annotated by BRENDA team
Bos taurus-2624--Manually annotated by BRENDA team
Brassica napusdifferent cultivars, gene pmi706204--Manually annotated by BRENDA team
Burkholderia cenocepaciastrain J2315, bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities690577--Manually annotated by BRENDA team
Burkholderia cepaciatype II enzyme, bifunctional protein with phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities671785Q06XM8SwissProtManually annotated by BRENDA team
Candida albicans-2817, 2818, 2820, 2822, 2828--Manually annotated by BRENDA team
Candida albicanswild-type and selenomethionine-labelled enzyme expressed in Escherichia coli2825--Manually annotated by BRENDA team
Cassia coluteoides-2813--Manually annotated by BRENDA team
Cavia porcellus-2624--Manually annotated by BRENDA team
Cyamopsis tetragonoloba-2813--Manually annotated by BRENDA team
Enterobacter aerogenes-2624--Manually annotated by BRENDA team
Escherichia coli-2818, 2829, 3354, 660706, 661902, 663077, 663078, 663079, 663166, 702663, 716883--Manually annotated by BRENDA team
Escherichia coliexpression in Brassica rapa681607, 682359--Manually annotated by BRENDA team
Escherichia coliexpression in Linum usitatissimum682360--Manually annotated by BRENDA team
Escherichia coliexpression in Malus domestica682353--Manually annotated by BRENDA team
Escherichia coliexpression in onion682354--Manually annotated by BRENDA team
Geobacillus thermodenitrificans-701812, 702817--Manually annotated by BRENDA team
Glycine max-2813--Manually annotated by BRENDA team
Homo sapiens-2624, 2817, 2821, 2826, 2828, 681498, 716883--Manually annotated by BRENDA team
Leishmania mexicana-652215Q9GRS9SwissProtManually annotated by BRENDA team
Mammalia-2624--Manually annotated by BRENDA team
Microorganisms-2624--Manually annotated by BRENDA team
Mus musculus-662458--Manually annotated by BRENDA team
Nakazawaea holstii-2624--Manually annotated by BRENDA team
Oncidium Gower Ramsey-716507--Manually annotated by BRENDA team
Oryctolagus cuniculus-2624--Manually annotated by BRENDA team
Ovis aries-2624--Manually annotated by BRENDA team
Photorhabdus luminescens-713855--Manually annotated by BRENDA team
Photorhabdus luminescens TT01-713855--Manually annotated by BRENDA team
Placopecten magellanicus-705394--Manually annotated by BRENDA team
Pseudomonas aeruginosa-2624, 2814, 3354, 661119--Manually annotated by BRENDA team
Pseudomonas aeruginosabifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase2823, 2824--Manually annotated by BRENDA team
Pseudomonas aeruginosastrain PAO1. Bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities692361--Manually annotated by BRENDA team
Pseudomonas aeruginosa PAO1.strain PAO1. Bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities692361--Manually annotated by BRENDA team
Pyrobaculum aerophilumbifunctional phosphoglucose isomerase/phosphomannose isomerase, EC 5.3.1.9 and 5.3.1.8, resp.662267Q8ZWV0UniprotManually annotated by BRENDA team
Pyrobaculum aerophilumbifunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.8 and EC 5.3.1.9, overexpression in Escherichia coli661679--Manually annotated by BRENDA team
Pyrobaculum aerophilumbiunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.660585--Manually annotated by BRENDA team
Pyrobaculum aerophilumbiunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.661100Q8ZWV0UniprotManually annotated by BRENDA team
Pyrococcus furiosusDSM 3638694521--Manually annotated by BRENDA team
Rattus norvegicus-2624, 2812--Manually annotated by BRENDA team
Saccharomyces cerevisiae-2624, 2806, 2807, 2811, 2816, 2817, 2828, 652637, 661119, 662318, 702663--Manually annotated by BRENDA team
Saccharomyces cerevisiaesecretory mutant with a thermolabile phosphomannose isomerase2819--Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium-690273--Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium-701472P25081UniProtManually annotated by BRENDA team
Sphingobium chungbukensestrain DJ77, gene pmi702869--Manually annotated by BRENDA team
Sphingobium chungbukense DJ77strain DJ77, gene pmi702869--Manually annotated by BRENDA team
Streptomyces nodosus-693999--Manually annotated by BRENDA team
Sulfolobus solfataricusstrain P1 (ATCC 35091)680450--Manually annotated by BRENDA team
Sulfolobus solfataricus P1strain P1 (ATCC 35091)680450--Manually annotated by BRENDA team
Sus scrofa-2624, 2817, 2828--Manually annotated by BRENDA team
Thermoplasma acidophilumbiunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.662220Q9HIC2SwissprotManually annotated by BRENDA team
Thermus thermophilus-713854--Manually annotated by BRENDA team
Thermus thermophilus-714372Q5SIM4UniProtManually annotated by BRENDA team
Thermus thermophilus KCCM 40879-713854--Manually annotated by BRENDA team
Thermus thermophilus KCCM 40879-714372Q5SIM4UniProtManually annotated by BRENDA team
Trigonella foenum-graecum-2813--Manually annotated by BRENDA team
Vigna angularis-693863--Manually annotated by BRENDA team
Xanthomonas campestris-2827--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
malfunctionAspergillus fumigatusQ66WM4uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview705568
malfunctionPhotorhabdus luminescens-the manA-deficient mutant is unable to utilize D-mannose as a sole carbon source713855
metabolismAlcaligenes sp.-the enzyme is part of the biosynthetic pathway of sugar nucleotides essential for welan gum production in Alcaligenes sp., overview701879
metabolismSphingobium chungbukense-phosphomannose isomerase catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate in the extracellular polysaccharide synthesis pathway, feedback regulation of this pathway702869
metabolismAspergillus fumigatusQ66WM4the enzyme catalyzes the first committed step in the synthesis of mannose-containing sugar chains and provides a link between glucose metabolism and mannosylation705568
physiological functionPhotorhabdus luminescens-phosphomannose isomerase has a major effect on the formation of a complete, branched extracellular polysaccharide. The manA gene influences biofilm maturation but not initial attachment713855

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-fructose 6-phosphatealpha-D-mannose 6-phosphate
show the reaction diagram		Pyrococcus furiosus--694521--r
beta-D-mannose 6-phosphatebeta-D-fructose 6-phosphate
show the reaction diagram		Escherichia coli, Homo sapiens--716883--r
D-AlloseD-Psicose
show the reaction diagram		Thermus thermophilus--713854--r
D-AlloseD-Psicose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
D-fructose 6-phosphateD-glucose 6-phosphate
show the reaction diagram		Aeropyrum pernixQ9YE01-662220--r
D-fructose 6-phosphateD-glucose 6-phosphate
show the reaction diagram		Thermoplasma acidophilumQ9HIC2-662220--r
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Escherichia coli--661902--r
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Pyrobaculum aerophilum--661679--r
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Leishmania mexicanaQ9GRS9-652215-652215r
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Aeropyrum pernixQ9YE01-662220--r
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Thermoplasma acidophilumQ9HIC2-662220--r
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Thermus thermophilusQ5SIM4-714372--r
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Leishmania mexicanaQ9GRS9first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates652215-652215r
D-Fructose 6-phosphate?
show the reaction diagram		Homo sapiens--2624---
D-Fructose 6-phosphate?
show the reaction diagram		Homo sapiens-first enzyme of the N-glycosylation pathway2821---
D-Fructose 6-phosphate?
show the reaction diagram		Microorganisms-mannose 6-phosphate produced in this manner can be incorporated via mannose 1-phosphate as intermediate into guanosine diphosphomannose which participates in numerous processes related to cell wall biosynthesis2624---
D-Fructose 6-phosphate?
show the reaction diagram		Escherichia coli-enzyme is involved in alginate biosynthesis3354---
D-glucose 6-phosphateD-fructose 6-phosphate
show the reaction diagram		Sulfolobus solfataricus--680450--?
D-glucose 6-phosphateD-fructose 6-phosphate
show the reaction diagram		Aeropyrum pernixQ9YE01-662220--r
D-glucose 6-phosphateD-fructose 6-phosphate
show the reaction diagram		Thermoplasma acidophilumQ9HIC2-662220--r
D-LyxoseD-Xylulose
show the reaction diagram		Thermus thermophilus--713854--r
D-LyxoseD-Xylulose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
D-LyxoseD-Xylulose
show the reaction diagram		Geobacillus thermodenitrificans-38% conversion yield after 3 h702817--?
D-MannoseD-Fructose
show the reaction diagram		Thermus thermophilus--713854--r
D-MannoseD-Fructose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Cavia porcellus, Mammalia--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Escherichia coli--2818-2818-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Escherichia coli--2829-2829-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Escherichia coli--3354-3354-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Escherichia coli--661902, 702663--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Homo sapiens--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Homo sapiens--2817-2817-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Homo sapiens--2821-2821-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Homo sapiens--2826-2826-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Homo sapiens--2828-2828-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Rattus norvegicus--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Rattus norvegicus--2812-2812-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Sus scrofa--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Sus scrofa--2817-2817-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Sus scrofa--2828-2828-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--2806-2806-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--2816-2816-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--2817-2817-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--2819-2819-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--2828-2828-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--661119--?
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae--702663--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Bos taurus, Oryctolagus cuniculus, Ovis aries--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Glycine max--2813-2813-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Arabidopsis thaliana--693149--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Enterobacter aerogenes, Pseudomonas aeruginosa--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Pseudomonas aeruginosa--2814-2814-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Pseudomonas aeruginosa--2823-2823-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Pseudomonas aeruginosa--2824-2824-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Pseudomonas aeruginosa--3354-3354-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Pseudomonas aeruginosa--661119--?
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Pseudomonas aeruginosa--692361--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Brassica napus--706204--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Ascaris suum, Apis mellifera--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Candida albicans--2817-2817-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Candida albicans--2818-2818-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Candida albicans--2820-2820-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Candida albicans--2822-2822-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Candida albicans--2825-2825-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Candida albicans--2828-2828-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Alcaligenes sp.--701879--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Xanthomonas campestris--2827-2827-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Nakazawaea holstii, Microorganisms--2624-2624-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Amorphophallus konjac--2809-2809-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Amorphophallus konjac--2810-2810-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Cassia coluteoides, Cyamopsis tetragonoloba, Trigonella foenum-graecum--2813-2813-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Sulfolobus solfataricus--680450--?
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Pyrobaculum aerophilum--661679--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Geobacillus thermodenitrificans--701812, 702817--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Aeropyrum pernixQ9YE01-662220--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Thermoplasma acidophilumQ9HIC2-662220--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Burkholderia cenocepacia--690577--?
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Burkholderia cepaciaQ06XM8-671785--?
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Sphingobium chungbukense--702869--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Salmonella enterica subsp. enterica serovar TyphimuriumP25081-701472--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Aspergillus fumigatusQ66WM4-705568--r
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae-beta-D-fructose 6-phosphate serves as substrate in the reverse direction2811-2811-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Saccharomyces cerevisiae-highly specific for the beta anomer of mannose 6-phosphate, the alpha anomer has no activity as a substrate, and is, at best, a poor inhibitor2807-2807-
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Thermus thermophilusQ5SIM4best substrate714372--r
D-Mannose 6-phosphate?
show the reaction diagram		Cassia coluteoides-enzyme is involved in the utilization of mannose released by hydrolysis of galactomannan on germination after phosphorylation to mannose 6-phosphate2813---
D-Mannose 6-phosphate?
show the reaction diagram		Mammalia-channeling D-mannose 6-phosphate into glycolysis by isomerization to fructose 6-phosphate2624---
D-RiboseD-Ribulose
show the reaction diagram		Thermus thermophilus--713854--r
D-RiboseD-Ribulose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
D-Ribose 5-phosphateD-Ribulose 5-phosphate
show the reaction diagram		Thermus thermophilusQ5SIM4very low activity714372--r
D-taloseD-tagatose
show the reaction diagram		Thermus thermophilus--713854--r
D-taloseD-tagatose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
L-alloseL-psicose
show the reaction diagram		Thermus thermophilus--713854--r
L-alloseL-psicose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
L-LyxoseL-Xylulose
show the reaction diagram		Thermus thermophilus--713854--r
L-LyxoseL-Xylulose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
L-MannoseL-Fructose
show the reaction diagram		Thermus thermophilus--713854--r
L-MannoseL-Fructose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
L-riboseL-ribulose
show the reaction diagram		Thermus thermophilus--713854--r
L-riboseL-ribulose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
L-riboseL-ribulose
show the reaction diagram		Geobacillus thermodenitrificans-29% conversion yield after 3 h702817--?
L-ribuloseL-ribose
show the reaction diagram		Thermus thermophilus-highest activity713854--r
L-ribuloseL-ribose
show the reaction diagram		Bacillus subtilisQ9AGZ4best substrate701797--r
L-taloseL-tagatose
show the reaction diagram		Thermus thermophilus--713854--r
L-taloseL-tagatose
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--r
additional information?-Homo sapiens--2624---
additional information?-Enterobacter aerogenes-constitutive enzyme2624---
additional information?-Candida albicans-enzyme is involved in biosynthesis of mannan components of the cell walls2818, 2820---
additional information?-Pseudomonas aeruginosa-adaptive enzyme2624---
additional information?-Homo sapiens-critical role in the supply of the D-mannose derivatives required for many glycosylation reactions2826---
additional information?-Candida albicans-reversible isomerization of mannose 6-phosphate and fructose 6-phosphate is the initial commited step in the synthesis of the mannosylated glycoproteins, which are essential in biosynthesis of functional fungal cell wall. Absence of mannose-6-phosphate isomerase causes cell lysis2822---
additional information?-Sulfolobus solfataricus-no catalytic activity toward glucosamine 6-phosphate or N-acetylglucosamine 6-phosphate680450---
additional information?-Geobacillus thermodenitrificans-enzyme substrate specificity with diverse monosaccharide aldoses and ketoses, overview702817---
additional information?-Escherichia coli, Saccharomyces cerevisiae-Molecular mechanics study of enzyme substrate and inhibitors, overview702663---
additional information?-Sphingobium chungbukense-PMI is bifunctional possessing both mannose 6-phosphate isomerase and GDP-mannose diphosphorylase activities702869---
additional information?-Bacillus subtilisQ9AGZ4the enzyme is specific for aldose substrates possessing hydroxyl groups oriented in the same direction at the C-2 and C-3 positions, such as the D- and L-enantiomers of ribose, lyxose, talose, mannose, and allose, substrate specificity, overview701797---
additional information?-Thermus thermophilusQ5SIM4no activity with D-glucose 6-phosphate and arabinose 5-phosphate714372---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
D-fructose 6-phosphateD-mannose 6-phosphate
show the reaction diagram		Leishmania mexicanaQ9GRS9first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates652215-652215
D-Fructose 6-phosphate?
show the reaction diagram		Homo sapiens--2624--
D-Fructose 6-phosphate?
show the reaction diagram		Homo sapiens-first enzyme of the N-glycosylation pathway2821--
D-Fructose 6-phosphate?
show the reaction diagram		Microorganisms-mannose 6-phosphate produced in this manner can be incorporated via mannose 1-phosphate as intermediate into guanosine diphosphomannose which participates in numerous processes related to cell wall biosynthesis2624--
D-Fructose 6-phosphate?
show the reaction diagram		Escherichia coli-enzyme is involved in alginate biosynthesis3354--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Escherichia coli, Saccharomyces cerevisiae--702663--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Brassica napus--706204--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Alcaligenes sp.--701879--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Geobacillus thermodenitrificans--701812, 702817--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Sphingobium chungbukense--702869--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Salmonella enterica subsp. enterica serovar TyphimuriumP25081-701472--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Bacillus subtilisQ9AGZ4-701797--
D-Mannose 6-phosphateD-Fructose 6-phosphate
show the reaction diagram		Aspergillus fumigatusQ66WM4-705568--
D-Mannose 6-phosphate?
show the reaction diagram		Cassia coluteoides-enzyme is involved in the utilization of mannose released by hydrolysis of galactomannan on germination after phosphorylation to mannose 6-phosphate2813--
D-Mannose 6-phosphate?
show the reaction diagram		Mammalia-channeling D-mannose 6-phosphate into glycolysis by isomerization to fructose 6-phosphate2624--
additional information?-Homo sapiens--2624--
additional information?-Enterobacter aerogenes-constitutive enzyme2624--
additional information?-Candida albicans-enzyme is involved in biosynthesis of mannan components of the cell walls2818, 2820--
additional information?-Pseudomonas aeruginosa-adaptive enzyme2624--
additional information?-Homo sapiens-critical role in the supply of the D-mannose derivatives required for many glycosylation reactions2826--
additional information?-Candida albicans-reversible isomerization of mannose 6-phosphate and fructose 6-phosphate is the initial commited step in the synthesis of the mannosylated glycoproteins, which are essential in biosynthesis of functional fungal cell wall. Absence of mannose-6-phosphate isomerase causes cell lysis2822--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ba2+Bacillus subtilisQ9AGZ4activates701797
Ca2+Pseudomonas aeruginosa-activates2824
Ca2+Xanthomonas campestris--2827
Ca2+Burkholderia cepaciaQ06XM8best activator, may be replaced by Mg2+ or Mn2+ for phosphomannose isomerase activity671785
Ca2+Salmonella enterica subsp. enterica serovar TyphimuriumP25081activates701472
Ca2+Bacillus subtilisQ9AGZ4activates701797
Ca2+Geobacillus thermodenitrificans-activates702817
Ca2+Sphingobium chungbukense-activates702869
Ca2+Thermus thermophilusQ5SIM4the enzyme is not stimulated by Ca2+714372
Co2+Saccharomyces cerevisiae-can reverse inhibition by EDTA2806
Co2+Amorphophallus konjac-can reverse inhibition by a metal binding agent2809
Co2+Pseudomonas aeruginosa-best activator2824
Co2+Xanthomonas campestris-activates2827
Co2+Pseudomonas aeruginosa-required for phosphomannose isomerase activity692361
Co2+Salmonella enterica subsp. enterica serovar TyphimuriumP25081activates701472
Co2+Bacillus subtilisQ9AGZ4activates, best metal ion, maximal activity at 0.5 mM701797
Co2+Geobacillus thermodenitrificans--701812
Co2+Geobacillus thermodenitrificans-activates, best activator metal ion702817
Co2+Sphingobium chungbukense-beste metal ion activator702869
Co2+Thermus thermophilus-about 230% activity at 0.5 mM713854, 714372
Cu2+Bacillus subtilisQ9AGZ4activates701797
Cu2+Geobacillus thermodenitrificans-activates702817
Cu2+Thermus thermophilus-maximal activity of the recombinant enzyme for L-ribulose isomerization in the presence of 0.5 mM Cu2+713854
Cu2+Thermus thermophilusQ5SIM4about 135% activity at 0.5 mM714372
Fe2+Saccharomyces cerevisiae-can reverse inhibition by EDTA2806
Fe2+Amorphophallus konjac-can reverse inhibition by a metal binding agent2809
Fe2+Geobacillus thermodenitrificans-activates702817
Fe2+Thermus thermophilusQ5SIM4about 125% activity at 0.5 mM714372
Mg2+Pseudomonas aeruginosa-activates2824
Mg2+Burkholderia cepaciaQ06XM860% of activity with Ca2+ for phosphomannose isomerase activity671785
Mg2+Salmonella enterica subsp. enterica serovar TyphimuriumP25081best activating divalent metal ion701472
Mg2+Bacillus subtilisQ9AGZ4activates701797
Mg2+Geobacillus thermodenitrificans-activates702817
Mg2+Sphingobium chungbukense-activates only the GMP activity of the enzyme702869
Mg2+Thermus thermophilusQ5SIM4about 175% activity at 0.5 mM714372
Mn2+Amorphophallus konjac-can reverse inhibition by a metal binding agent2809
Mn2+Pseudomonas aeruginosa-activates2824
Mn2+Xanthomonas campestris-activates2827
Mn2+Burkholderia cepaciaQ06XM865% of activity with Ca2+ for phosphomannose isomerase activity671785
Mn2+Salmonella enterica subsp. enterica serovar TyphimuriumP25081activates701472
Mn2+Bacillus subtilisQ9AGZ4highly activating701797
Mn2+Geobacillus thermodenitrificans-activates702817
Mn2+Thermus thermophilus-about 160% activity at 0.5 mM713854
Ni2+Pseudomonas aeruginosa-activates2824
Ni2+Xanthomonas campestris--2827
Ni2+Salmonella enterica subsp. enterica serovar TyphimuriumP25081activates701472
Ni2+Bacillus subtilisQ9AGZ4activates701797
Ni2+Geobacillus thermodenitrificans-activates702817
Ni2+Sphingobium chungbukense-activates702869
ZincSaccharomyces cerevisiae-contains 1 gatom per mol of enzyme2806
ZincCandida albicans-enzyme contains an essential zinc atom. Four of the five ligands come from the protein, one of these ligands is unique in that it is a glutamine2822
ZincPseudomonas aeruginosa-weak activation2824
ZincCandida albicans, Homo sapiens-recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins2828
ZincSaccharomyces cerevisiae--2828
Zn2+Saccharomyces cerevisiae-can reverse inhibition by EDTA2806
Zn2+Amorphophallus konjac-at low concentrations complete reactivation of enzyme inhibited by a metal binding agent2809
Zn2+Xanthomonas campestris-activates2827
Zn2+Escherichia coli-noncovalent complexation, ESI-FTICR study, binding/release of metal ion changes substrate binding affinity by at least 5fold660706
Zn2+Salmonella enterica subsp. enterica serovar TyphimuriumP25081enzyme-bound, Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site701472
Zn2+Bacillus subtilisQ9AGZ4activates701797
Zn2+Geobacillus thermodenitrificans-activates poorly702817
Zn2+Sphingobium chungbukense-activates702869
Zn2+Aspergillus fumigatusQ66WM4-705568
Zn2+Thermus thermophilus-about 130% activity at 0.5 mM713854
Zn2+Thermus thermophilusQ5SIM4Zn2+ is present at one molecule per monomer, the enzyme has about 240% activity in the presence of 0.5 mM Zn2+714372
Zn2+Escherichia coli, Homo sapiens-zinc-dependent metalloenzyme716883
Mn2+Thermus thermophilusQ5SIM4about 175% activity at 0.5 mM714372
additional informationPseudomonas aeruginosa-activated by bivalent cations in the order: Co2+, Ni2+, Mn2+, Mg2+, Ca2+, Zn2+2824
additional informationXanthomonas campestris-activated by bivalent cations in decreasing order: Co2+, Zn2+, Mn2+, Ni2+, Ca2+2827
additional informationSalmonella enterica subsp. enterica serovar TyphimuriumP25081divalent cations are absolutely required for activity, metal binding increases the thermostability of the enzyme701472
additional informationBacillus subtilisQ9AGZ4mannose-6-phosphate isomerases are metalloenzymes that require a divalent ion metal cofactor for activity and catalysis701797
additional informationGeobacillus thermodenitrificans-the enzyme requires divalent cations for activity702817
additional informationSphingobium chungbukense-PMI absolutely requires divalent metal cations for catalytic activity702869
additional informationThermus thermophilus-the enzyme is not affected by Ca2+, Mg2+, Ba2+, and Ni2+713854

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.000041 {5-phospho-D-arabinonohydroxamic acid}Homo sapiens-in 50 mM HEPES buffer, pH 7.1, at 25°C716883-
0.0006 {5-phospho-D-arabinonhydrazide}Homo sapiens-in 50 mM HEPES buffer, pH 7.1, at 25°C716883-
1,10-phenanthrolineSaccharomyces cerevisiae--2806, 2828 2D-image
1,10-phenanthrolineAmorphophallus konjac--2809, 2810 2D-image
1,10-phenanthrolineCandida albicans, Homo sapiens, Sus scrofa--2828 2D-image
2,2'-dipyridylSaccharomyces cerevisiae--2806 2D-image
2,2'-dipyridylAmorphophallus konjac--2810 2D-image
2,3-ButanedionePseudomonas aeruginosa-inactivation692361 2D-image
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactoneEscherichia coli, Saccharomyces cerevisiae--702663-
5-deoxy-5-phosphonomethyl-D-arabinonateEscherichia coli, Saccharomyces cerevisiae--702663-
5-deoxy-5-phosphonomethyl-D-arabinonohydrazideEscherichia coli, Saccharomyces cerevisiae--702663-
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acidEscherichia coli, Saccharomyces cerevisiae--702663-
5-phospho-D-arabinonhydrazideEscherichia coli, Homo sapiens--716883 2D-image
5-phospho-D-arabinonohydroxamic acidPseudomonas aeruginosa-50% inhibition at 0.000169 mM, inhibition of both type I and type II isozymes661119 2D-image
5-phospho-D-arabinonohydroxamic acidSaccharomyces cerevisiae-50% inhibition at 0.000136 mM, inhibition of both type I and type II isozymes661119 2D-image
5-phospho-D-arabinonohydroxamic acidEscherichia coli, Homo sapiens-nanomolar inhibitor716883 2D-image
5-phosphoarabinonatePyrobaculum aerophilumQ8ZWV0-662267 2D-image
6-deoxy-6-carboxymethyl-D-mannoseEscherichia coli, Saccharomyces cerevisiae--702663-
6-deoxy-6-dicarboxymethyl-D-mannoseEscherichia coli, Saccharomyces cerevisiae--702663-
6-deoxy-6-dimethylmalonate-D-mannopyranoseEscherichia coli, Saccharomyces cerevisiae--702663-
6-deoxy-6-phosphonomethyl-D-mannoseEscherichia coli, Saccharomyces cerevisiae--702663-
6-phospho-2-deoxygluconateCassia coluteoides-competitive2813 2D-image
6-phosphogluconateSaccharomyces cerevisiae-competitive2624 2D-image
6-phosphogluconateCassia coluteoides-slight inhibition2813 2D-image
6-phosphogluconatePyrobaculum aerophilum--661679 2D-image
6-phosphogluconateAeropyrum pernixQ9YE01-662220 2D-image
6-phosphogluconateThermoplasma acidophilumQ9HIC2-662220 2D-image
6-PhosphomannonateCassia coluteoides-competitive2813 2D-image
8-hydroxyquinolineSaccharomyces cerevisiae--2806 2D-image
ADP-glucosePseudomonas aeruginosa-0.5 mM, 77.8% of initial activity692361 2D-image
Ag+Candida albicans-irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme2818 2D-image
alpha-D-Mannose 6-phosphateSaccharomyces cerevisiae-poor2807 2D-image
Arabinose 5-phosphateCandida albicans, Homo sapiens, Saccharomyces cerevisiae, Sus scrofa--2828 2D-image
Ba2+Thermus thermophilusQ5SIM4about 30% inhibition at 0.5 mM714372 2D-image
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranosideEscherichia coli, Saccharomyces cerevisiae--702663-
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannoseEscherichia coli, Saccharomyces cerevisiae--702663-
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannoseEscherichia coli, Saccharomyces cerevisiae--702663-
Cd2+Saccharomyces cerevisiae-competitive, strongly pH dependent2816 2D-image
Cd2+Candida albicans--2825 2D-image
Cd2+Arabidopsis thaliana-1 mM, no residual activity693149 2D-image
cysteineSaccharomyces cerevisiae--2806 2D-image
D-mannose 1-phosphatePseudomonas aeruginosa-0.5 mM, 81.9% of initial activity692361 2D-image
DiethyldicarbonateXanthomonas campestris--2827 2D-image
dithiothreitolSaccharomyces cerevisiae--2806, 2828 2D-image
dithiothreitolPseudomonas aeruginosa--2824 2D-image
dithiothreitolCandida albicans, Homo sapiens, Sus scrofa--2828 2D-image
dithiothreitolArabidopsis thaliana-1 mM, 73% residual activity; 1 mM, 84% residual activity693149 2D-image
EDTASaccharomyces cerevisiae--2806, 2828 2D-image
EDTAAmorphophallus konjac--2809, 2810 2D-image
EDTACandida albicans, Homo sapiens, Sus scrofa--2828 2D-image
EDTABurkholderia cepaciaQ06XM82 mM, complete inhibition671785 2D-image
EDTAArabidopsis thaliana-2.5 mM, 54% residual activity; 2.5 mM, 86% residual activity693149 2D-image
EDTASalmonella enterica subsp. enterica serovar TyphimuriumP25081complete inhibition at 1 mM, reversible by the addition of divalent metal cations such as Zn2+, Mn2+, Co2+, Mg2+ and Ni2+701472 2D-image
EDTABacillus subtilisQ9AGZ4complete inactivation701797 2D-image
EDTAGeobacillus thermodenitrificans-strong inhibition702817 2D-image
EDTAThermus thermophilus-about 75% residual activity at 0.5 mM713854 2D-image
EDTAThermus thermophilusQ5SIM4complete inhibition at 0.5 mM714372 2D-image
erythrose 4-phosphateHomo sapiens, Sus scrofa--2624, 2828 2D-image
erythrose 4-phosphateSaccharomyces cerevisiae-; competitive2624 2D-image
erythrose 4-phosphateCassia coluteoides-D-erythrose 4-phosphate, competitive2813 2D-image
erythrose 4-phosphateCandida albicans, Saccharomyces cerevisiae--2828 2D-image
erythrose 4-phosphateEscherichia coli--660706 2D-image
erythrose 4-phosphatePyrobaculum aerophilum--661679 2D-image
erythrose 4-phosphateAeropyrum pernixQ9YE01-662220 2D-image
erythrose 4-phosphateThermoplasma acidophilumQ9HIC2-662220 2D-image
Fe2+Thermus thermophilus-12% residual activity at 0.5 mM713854 2D-image
fructose 1-phosphateHomo sapiens-competitive2821 2D-image
Galactose 6-hosphateSaccharomyces cerevisiae-competitive2624-
GDP-D-mannoseSphingobium chungbukense-inhibits mannose 6-phosphate isomerase activity of PMI, feedback regulation of this pathway702869 2D-image
GDP-mannosePseudomonas aeruginosa-0.5 mM, 46.7% of initial activity692361 2D-image
glucosamine 6-phosphateSaccharomyces cerevisiae-competitive2624 2D-image
glucose 1-phosphateSaccharomyces cerevisiae-competitive2624 2D-image
glucose 6-phosphateSaccharomyces cerevisiae-competitive2624 2D-image
Hg2+Saccharomyces cerevisiae-competitive, relatively pH-independent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion2816 2D-image
Hg2+Candida albicans-partial noncompetitive inhibition with mannose 6-phosphate as substrate. In addition to the inhibition at rapid equilibrium, inactivation occurs in a two-step process, proceeding via an intermediate complex. The rate of the irreversible inactivation can be slowed by the addition of the substrate mannose 6-phosphate2817 2D-image
Hg2+Saccharomyces cerevisiae--2817 2D-image
Hg2+Candida albicans-recombinant wild-type enzyme and selenomethionine-labelled enzyme2825 2D-image
HgCl2Amorphophallus konjac--2809 2D-image
KI-VALUEHomo sapiens--716883-
L-ascorbic acidArabidopsis thaliana-1 mM, 77% residual activity693149 2D-image
mannitol 1-phosphateSaccharomyces cerevisiae-competitive2624 2D-image
mannitol 1-phosphateCassia coluteoides-competitive2813 2D-image
p-chloromercuribenzoateArabidopsis thaliana-0.05 mM, 33% residual activity; 0.05 mM, 39% residual activity693149 2D-image
PCMBAmorphophallus konjac--2809 2D-image
phosphateSaccharomyces cerevisiae-competitive2624 2D-image
ribose 5-phosphateSaccharomyces cerevisiae-competitive2624 2D-image
S-nitroso-acetyl-penicillamineSaccharomyces cerevisiae-dose- and time-dependent inactivation652637 2D-image
Silver sulfadiazineCandida albicans-wild-type enzyme is inhibited, mutant enzyme Cys150Ala is not inhibited2818 2D-image
Silver sulfadiazineEscherichia coli-no inhibition2818 2D-image
sorbitol 6-phosphateSaccharomyces cerevisiae-competitive2624 2D-image
yttriumSalmonella enterica subsp. enterica serovar TyphimuriumP25081-701472-
Zn2+Saccharomyces cerevisiae-competitive with mannose 6-phosphate, strongly pH-dependent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion2816 2D-image
Zn2+Candida albicans--2825 2D-image
Zn2+Burkholderia cenocepacia-inhibitory to both phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities690577 2D-image
Zn2+Arabidopsis thaliana-1 mM, no residual activity693149 2D-image
mannitol 1-phosphateEscherichia coli--660706 2D-image
additional informationSaccharomyces cerevisiae-no inhibition by N-acetyl-penicillamine652637-
additional informationPseudomonas aeruginosa, Saccharomyces cerevisiae-not inhibitory: 5-phospho-D-arabinonate661119-
additional informationBurkholderia cepaciaQ06XM8not inhibitory: mannose 1-phosphate, GTP, GDP-mannose, or diphosphate671785-
additional informationEscherichia coli-synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive enzyme inhibitors. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview702663-
additional informationSaccharomyces cerevisiae-synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive inhibitors of the enzyme. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview702663-
additional informationSphingobium chungbukense-no inhibition by GTP, mannose 1-phosphate, and phosphodiphosphate702869-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Ca2+Burkholderia cenocepacia-order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+690577 2D-image
Co2+Burkholderia cenocepacia-order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+690577 2D-image
diphosphatePseudomonas aeruginosa-0.5 mM, 120% of initial activity692361 2D-image
Mg2+Burkholderia cenocepacia-order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+690577 2D-image
Mn2+Burkholderia cenocepacia-Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+690577 2D-image
Ni2+Burkholderia cenocepacia-order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+690577 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00043-beta-D-mannose 6-phosphateHomo sapiens-in 50 mM HEPES buffer, pH 7.1, at 25°C716883-
0.33-beta-D-mannose 6-phosphateEscherichia coli-in 50 mM HEPES buffer, pH 7.1, at 25°C716883-
0.06-D-fructose 6-phosphatePyrobaculum aerophilum-pH 7.4, 80°C661679 2D-image
0.15-D-fructose 6-phosphateEscherichia coli-22°C, pH 7.4661902 2D-image
0.2-D-fructose 6-phosphateThermoplasma acidophilumQ9HIC280°C, pH 7.4662220 2D-image
0.21-D-fructose 6-phosphateAeropyrum pernixQ9YE0150°C, pH 7.4662220 2D-image
0.22-D-fructose 6-phosphateThermus thermophilusQ5SIM4wild type enzyme, pH 7.0, 80°C714372 2D-image
0.3-D-fructose 6-phosphatePyrobaculum aerophilum-pH 7.4, 50°C661679 2D-image
0.44-D-fructose 6-phosphateAeropyrum pernixQ9YE0180°C, pH 7.4662220 2D-image
0.002-D-glucose 6-phosphateSulfolobus solfataricus-mutant enzyme S309D, at 65°C680450 2D-image
0.006-D-glucose 6-phosphateSulfolobus solfataricus-mutant enzyme S309Q, at 65°C680450 2D-image
0.008-D-glucose 6-phosphateSulfolobus solfataricus-mutant enzyme S309N, at 65°C; mutant enzyme S309T, at 65°C680450 2D-image
0.009-D-glucose 6-phosphateSulfolobus solfataricus-mutant enzyme S309A, at 65°C680450 2D-image
0.012-D-glucose 6-phosphateSulfolobus solfataricus-mutant enzyme S309V, at 65°C680450 2D-image
0.013-D-glucose 6-phosphateSulfolobus solfataricus-wild type enzyme, at 65°C680450 2D-image
0.72-D-glucose 6-phosphateThermoplasma acidophilumQ9HIC280°C, pH 7.4662220 2D-image
3.5-D-glucose 6-phosphateAeropyrum pernixQ9YE0180°C, pH 7.4662220 2D-image
433-D-LyxoseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
946-D-mannoseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
0.0413-D-mannose 6-phosphateArabidopsis thaliana-pH 7.5, 25°C693149 2D-image
0.06-D-mannose 6-phosphatePyrobaculum aerophilum-pH 7.4, 80°C661679 2D-image
0.121-D-mannose 6-phosphateSaccharomyces cerevisiae-pH 7.1, 25°C661119 2D-image
0.18-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme E132A, pH 7.0, 80°C; mutant enzyme E67A, pH 7.0, 80°C714372 2D-image
0.21-D-mannose 6-phosphateThermus thermophilusQ5SIM4wild type enzyme, pH 7.0, 80°C714372 2D-image
0.25-D-mannose 6-phosphateThermoplasma acidophilumQ9HIC280°C, pH 7.4662220 2D-image
0.27-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme H122A, pH 7.0, 80°C714372 2D-image
0.33-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme H50A, pH 7.0, 80°C714372 2D-image
0.372-D-mannose 6-phosphateArabidopsis thaliana-pH 7.5, 25°C693149 2D-image
0.53-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme Q48A, pH 7.0, 80°C714372 2D-image
0.85-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme W13A, pH 7.0, 80°C714372 2D-image
1.1-D-mannose 6-phosphateAeropyrum pernixQ9YE0180°C, pH 7.4662220 2D-image
1.18-D-mannose 6-phosphatePseudomonas aeruginosa-wild-type, pH 7.0, 25°C692361 2D-image
1.21-D-mannose 6-phosphateEscherichia coli-22°C, pH 7.4661902 2D-image
1.29-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme R142A, pH 7.0, 80°C714372 2D-image
2.5-D-mannose 6-phosphatePseudomonas aeruginosa-pH 7.1, 25°C661119 2D-image
9-D-mannose 6-phosphateBurkholderia cepaciaQ06XM8pH 7.6, presence of 5 mM Mg2+671785 2D-image
9.04-D-mannose 6-phosphatePseudomonas aeruginosa-mutant E410A, pH 7.0, 25°C692361 2D-image
12.28-D-mannose 6-phosphatePseudomonas aeruginosa-mutant R479A, pH 7.0, 25°C692361 2D-image
12.36-D-mannose 6-phosphatePseudomonas aeruginosa-mutant E458A, pH 7.0, 25°C692361 2D-image
12.4-D-mannose 6-phosphateBurkholderia cenocepacia-30°C, pH 7.6690577 2D-image
12.9-D-mannose 6-phosphatePseudomonas aeruginosa-mutant N433A, pH 7.0, 25°C692361 2D-image
15.9-D-mannose 6-phosphatePseudomonas aeruginosa-mutant R373A, pH 7.0, 25°C692361 2D-image
16.26-D-mannose 6-phosphatePseudomonas aeruginosa-mutant H411A, pH 7.0, 25°C692361 2D-image
23.12-D-mannose 6-phosphatePseudomonas aeruginosa-mutant R472A, pH 7.0, 25°C692361 2D-image
110-D-RiboseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
469-D-taloseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
312-L-alloseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
998-L-riboseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
136-L-ribuloseThermus thermophilus-wild type enzyme, at pH 7.0 and 75°C713854 2D-image
140-L-ribuloseThermus thermophilus-mutant enzyme R142N, at pH 7.0 and 75°C713854 2D-image
150-L-ribuloseThermus thermophilus-mutant enzyme R142Q, at pH 7.0 and 75°C713854 2D-image
151-L-ribuloseThermus thermophilus-mutant enzyme R142E, at pH 7.0 and 75°C713854 2D-image
184-L-ribuloseThermus thermophilus-mutant enzyme R142A, at pH 7.0 and 75°C713854 2D-image
228-L-ribuloseThermus thermophilus-mutant enzyme R142K, at pH 7.0 and 75°C713854 2D-image
308-L-ribuloseThermus thermophilus-mutant enzyme R142Y, at pH 7.0 and 75°C713854 2D-image
0.17-mannose 6-phosphateSus scrofa--2828 2D-image
0.2-mannose 6-phosphateCandida albicans-Hepes buffer2825 2D-image
0.23-mannose 6-phosphateHomo sapiens-recombinant enzyme2826 2D-image
0.25-mannose 6-phosphateHomo sapiens-wild-type enzyme2826, 2828 2D-image
0.65-mannose 6-phosphateSaccharomyces cerevisiae--2828 2D-image
0.73-mannose 6-phosphateAmorphophallus konjac--2810 2D-image
0.8-mannose 6-phosphateCandida albicans-selenomethionine-labelled enzyme, Hepes buffer2825 2D-image
1-mannose 6-phosphateCandida albicans-Tris/HCl buffer2825 2D-image
1.24-mannose 6-phosphateCandida albicans--2828 2D-image
1.35-mannose 6-phosphateSaccharomyces cerevisiae--2624 2D-image
1.6-mannose 6-phosphateCassia coluteoides-enzyme from developing seeds2813 2D-image
1.9-mannose 6-phosphateCassia coluteoides-enzyme from germinating seeds2813 2D-image
2-mannose 6-phosphateXanthomonas campestris--2827 2D-image
3.03-mannose 6-phosphatePseudomonas aeruginosa-bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase2824 2D-image
4-mannose 6-phosphateCandida albicans-selenomethionine-labelled enzyme, Tris/HCl buffer2825 2D-image
additional information-additional informationGeobacillus thermodenitrificans-enzyme kinetics with D-lyxose and L-ribose, overview702817-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
36beta-D-mannose 6-phosphateHomo sapiens-in 50 mM HEPES buffer, pH 7.1, at 25°C716883-
23-beta-D-mannose 6-phosphateEscherichia coli-in 50 mM HEPES buffer, pH 7.1, at 25°C716883-
141-D-fructose 6-phosphateThermus thermophilusQ5SIM4wild type enzyme, pH 7.0, 80°C714372 2D-image
7089-D-LyxoseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
3748-D-mannoseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
0.076-D-mannose 6-phosphatePseudomonas aeruginosa-pH 7.1, 25°C661119 2D-image
0.25-D-mannose 6-phosphatePseudomonas aeruginosa-mutant R472A, pH 7.0, 25°C692361 2D-image
0.54-D-mannose 6-phosphatePseudomonas aeruginosa-mutant R479A, pH 7.0, 25°C692361 2D-image
0.75-D-mannose 6-phosphatePseudomonas aeruginosa-mutant R373A, pH 7.0, 25°C692361 2D-image
1.38-D-mannose 6-phosphatePseudomonas aeruginosa-wild-type, pH 7.0, 25°C692361 2D-image
2.63-D-mannose 6-phosphatePseudomonas aeruginosa-mutant E410A, pH 7.0, 25°C692361 2D-image
3.25-D-mannose 6-phosphatePseudomonas aeruginosa-mutant E458A, pH 7.0, 25°C692361 2D-image
3.5-D-mannose 6-phosphatePseudomonas aeruginosa-mutant N433A, pH 7.0, 25°C692361 2D-image
4.41-D-mannose 6-phosphatePseudomonas aeruginosa-mutant H411A, pH 7.0, 25°C692361 2D-image
11-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme W13A, pH 7.0, 80°C714372 2D-image
19-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme E132A, pH 7.0, 80°C714372 2D-image
19.4-D-mannose 6-phosphateBurkholderia cepaciaQ06XM8pH 7.6, presence of 5 mM Mg2+671785 2D-image
20-D-mannose 6-phosphateSaccharomyces cerevisiae-pH 7.1, 25°C661119 2D-image
31-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme E67A, pH 7.0, 80°C714372 2D-image
37-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme Q48A, pH 7.0, 80°C714372 2D-image
54-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme H50A, pH 7.0, 80°C714372 2D-image
70-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme R142A, pH 7.0, 80°C714372 2D-image
75-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme H122A, pH 7.0, 80°C714372 2D-image
1371-D-mannose 6-phosphateThermus thermophilusQ5SIM4wild type enzyme, pH 7.0, 80°C714372 2D-image
72-D-RiboseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
63970-D-taloseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
920-L-alloseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
17600-L-riboseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797 2D-image
32670-L-ribuloseThermus thermophilus-mutant enzyme R142E, at pH 7.0 and 75°C713854 2D-image
48300-L-ribuloseThermus thermophilus-mutant enzyme R142Q, at pH 7.0 and 75°C713854 2D-image
50640-L-ribuloseThermus thermophilus-wild type enzyme, at pH 7.0 and 75°C713854 2D-image
56180-L-ribuloseThermus thermophilus-mutant enzyme R142Y, at pH 7.0 and 75°C713854 2D-image
64870-L-ribuloseThermus thermophilus-mutant enzyme R142A, at pH 7.0 and 75°C713854 2D-image
68880-L-ribuloseThermus thermophilus-mutant enzyme R142K, at pH 7.0 and 75°C713854 2D-image
81060-L-ribuloseThermus thermophilus-mutant enzyme R142N, at pH 7.0 and 75°C713854 2D-image
121-mannose 6-phosphateCandida albicans-selenomethionine-labelled enzyme2825 2D-image
162-mannose 6-phosphateCandida albicans-wild-type enzyme2825 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
70-beta-D-mannose 6-phosphateEscherichia coli-in 50 mM HEPES buffer, pH 7.1, at 25°C7168830
840-beta-D-mannose 6-phosphateHomo sapiens-in 50 mM HEPES buffer, pH 7.1, at 25°C7168830
641-D-fructose 6-phosphateThermus thermophilusQ5SIM4wild type enzyme, pH 7.0, 80°C7143729143
16.4-D-LyxoseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme7017979268
3.5-D-mannoseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme7017979286
13-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme W13A, pH 7.0, 80°C7143729288
54-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme R142A, pH 7.0, 80°C7143729288
69-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme Q48A, pH 7.0, 80°C7143729288
109-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme E132A, pH 7.0, 80°C7143729288
166-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme H50A, pH 7.0, 80°C7143729288
174-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme E67A, pH 7.0, 80°C7143729288
278-D-mannose 6-phosphateThermus thermophilusQ5SIM4mutant enzyme H122A, pH 7.0, 80°C7143729288
6685-D-mannose 6-phosphateThermus thermophilusQ5SIM4wild type enzyme, pH 7.0, 80°C7143729288
0.6-D-RiboseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme7017979348
6.8-D-taloseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme7017979377
2.9-L-alloseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme701797271994
17.6-L-riboseBacillus subtilisQ9AGZ4pH 7.5, 40°C, recombinant enzyme70179780181
182-L-ribuloseThermus thermophilus-mutant enzyme R142Y, at pH 7.0 and 75°C71385412394
216-L-ribuloseThermus thermophilus-mutant enzyme R142E, at pH 7.0 and 75°C71385412394
302-L-ribuloseThermus thermophilus-mutant enzyme R142K, at pH 7.0 and 75°C71385412394
322-L-ribuloseThermus thermophilus-mutant enzyme R142Q, at pH 7.0 and 75°C71385412394
353-L-ribuloseThermus thermophilus-mutant enzyme R142A, at pH 7.0 and 75°C71385412394
374-L-ribuloseThermus thermophilus-wild type enzyme, at pH 7.0 and 75°C71385412394
579-L-ribuloseThermus thermophilus-mutant enzyme R142N, at pH 7.0 and 75°C71385412394

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0006-5-phospho-D-arabinonhydrazideHomo sapiens-in 50 mM HEPES buffer, pH 7.1, at 25°C716883 2D-image
0.002-5-phospho-D-arabinonhydrazideEscherichia coli-in 50 mM HEPES buffer, pH 7.1, at 25°C716883 2D-image
4.1e-05-5-phospho-D-arabinonohydroxamic acidHomo sapiens-in 50 mM HEPES buffer, pH 7.1, at 25°C716883 2D-image
8e-05-5-phospho-D-arabinonohydroxamic acidEscherichia coli-in 50 mM HEPES buffer, pH 7.1, at 25°C716883 2D-image
8.6e-05-5-phospho-D-arabinonohydroxamic acidSaccharomyces cerevisiae-pH 7.1, 25°C661119 2D-image
0.000137-5-phospho-D-arabinonohydroxamic acidPseudomonas aeruginosa-pH 7.1, 25°C661119 2D-image
0.0105-6-deoxy-6-dicarboxymethyl-D-mannoseSaccharomyces cerevisiae-pH 7.1, 25°C, recombinant enzyme702663-
0.115-6-deoxy-6-dicarboxymethyl-D-mannoseEscherichia coli-pH 7.1, 25°C, recombinant enzyme702663-
0.11-6-phosphogluconatePyrobaculum aerophilum-pH 7.4, 50°C661679 2D-image
2106-phosphogluconateThermoplasma acidophilumQ9HIC280°C, pH 7.4662220 2D-image
58-6-phosphogluconateAeropyrum pernixQ9YE0180°C, pH 7.4662220 2D-image
0.035-erythrose 4-phosphateAeropyrum pernixQ9YE0180°C, pH 7.4662220 2D-image
0.164-erythrose 4-phosphateThermoplasma acidophilumQ9HIC280°C, pH 7.4662220 2D-image
0.0014-erythrose-4-phosphatePyrobaculum aerophilum-pH 7.4, 50°C661679 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3-5-deoxy-5-phosphonomethyl-D-arabinonate, 5-deoxy-5-phosphonomethyl-D-arabinonohydrazideEscherichia coli-above, pH 7.1, 25°C, recombinant enzyme702663-
0.37-5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acidEscherichia coli-pH 7.1, 25°C, recombinant enzyme702663-
2.2-5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acidSaccharomyces cerevisiae-pH 7.1, 25°C, recombinant enzyme702663-
0.9-6-deoxy-6-carboxymethyl-D-mannoseSaccharomyces cerevisiae-pH 7.1, 25°C, recombinant enzyme702663-
4.6-6-deoxy-6-carboxymethyl-D-mannoseEscherichia coli-pH 7.1, 25°C, recombinant enzyme702663-
0.0181-6-deoxy-6-dicarboxymethyl-D-mannoseSaccharomyces cerevisiae-pH 7.1, 25°C, recombinant enzyme702663-
0.199-6-deoxy-6-dicarboxymethyl-D-mannoseEscherichia coli-pH 7.1, 25°C, recombinant enzyme702663-
1.61-6-deoxy-6-phosphonomethyl-D-mannoseSaccharomyces cerevisiae-pH 7.1, 25°C, recombinant enzyme702663-
4.7-6-deoxy-6-phosphonomethyl-D-mannoseEscherichia coli-pH 7.1, 25°C, recombinant enzyme702663-

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.01-Thermus thermophilusQ5SIM4wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80°C714372
0.0101-Bacillus subtilisQ9AGZ4recombinant enzyme701797
0.0165-Bacillus subtilisQ9AGZ4recombinant enzyme701797
0.0225-Bacillus subtilisQ9AGZ4recombinant enzyme701797
0.0659-Bacillus subtilisQ9AGZ4recombinant enzyme701797
0.0918-Bacillus subtilisQ9AGZ4recombinant enzyme701797
0.269-Alcaligenes sp.-enzyme activity in cells after 54 h growth on maltose701879
0.3-Thermus thermophilusQ5SIM4mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
0.306-Alcaligenes sp.-enzyme activity in cells after 54 h growth on sucrose701879
0.313-Alcaligenes sp.-enzyme activity in cells after 54 h growth on glucose701879
0.6-Thermus thermophilusQ5SIM4mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
0.74-Thermus thermophilusQ5SIM4wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80°C714372
1.4-Thermus thermophilusQ5SIM4mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
1.5-Thermus thermophilusQ5SIM4mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
1.7-Thermus thermophilusQ5SIM4mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
1.9-Thermus thermophilusQ5SIM4mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
2.1-Thermus thermophilusQ5SIM4mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
2.8-Thermus thermophilusQ5SIM4mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
38Thermus thermophilusQ5SIM4mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
3-Thermus thermophilus-wild type enzyme, using D-psicose as substrate, at pH 7.0 and 75°C713854
4.5-Thermus thermophilusQ5SIM4wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80°C714372
5.95-Amorphophallus konjac--2810
11-Thermus thermophilusQ5SIM4mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
16-Thermus thermophilus-wild type enzyme, using L-tagatose as substrate, at pH 7.0 and 75°C713854
16-Thermus thermophilusQ5SIM4mutant enzyme K37A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
19-Thermus thermophilus-wild type enzyme, using L-mannose as substrate, at pH 7.0 and 75°C713854
22-Thermus thermophilus-wild type enzyme, using L-xylulose as substrate, at pH 7.0 and 75°C713854
23-Thermus thermophilus-wild type enzyme, using L-lyxose as substrate, at pH 7.0 and 75°C713854
31-Thermus thermophilusQ5SIM4mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
33.5-Xanthomonas campestris--2827
39-Thermus thermophilusQ5SIM4mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
40-Thermus thermophilusQ5SIM4mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
42-Thermus thermophilus-wild type enzyme, using L-psicose as substrate, at pH 7.0 and 75°C713854
44-Thermus thermophilusQ5SIM4mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
51-Thermus thermophilusQ5SIM4mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
57-Thermus thermophilus-wild type enzyme, using L-fructose as substrate, at pH 7.0 and 75°C713854
58-Thermus thermophilus-wild type enzyme, using D-ribose as substrate, at pH 7.0 and 75°C713854
58-Thermus thermophilusQ5SIM4mutant enzyme L18A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
63-Thermus thermophilus-wild type enzyme, using L-talose as substrate, at pH 7.0 and 75°C713854
75-Homo sapiens--2828
75-Thermus thermophilusQ5SIM4wild type enzyme, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
80-Sus scrofa--2828
85-Thermus thermophilus-wild type enzyme, using D-tagatose as substrate, at pH 7.0 and 75°C713854
126-Thermus thermophilus-wild type enzyme, using D-ribulose as substrate, at pH 7.0 and 75°C713854
128-Thermus thermophilus-wild type enzyme, using D-xylulose as substrate, at pH 7.0 and 75°C713854
165-Thermus thermophilus-wild type enzyme, using D-allose as substrate, at pH 7.0 and 75°C713854
167-Thermus thermophilus-wild type enzyme, using D-fructose as substrate, at pH 7.0 and 75°C713854
194-Thermus thermophilusQ5SIM4mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C714372
333-Thermus thermophilus-wild type enzyme, using D-lyxose as substrate, at pH 7.0 and 75°C713854
380-Candida albicans--2828
420-Saccharomyces cerevisiae--2828
425-Thermus thermophilus-wild type enzyme, using L-ribose as substrate, at pH 7.0 and 75°C713854
474-Thermus thermophilus-mutant enzyme K37A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
742-Thermus thermophilus-wild type enzyme, using L-allose as substrate, at pH 7.0 and 75°C713854
838-Thermus thermophilus-mutant enzyme W13A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
842-Thermus thermophilus-wild type enzyme, using D-mannose as substrate, at pH 7.0 and 75°C713854
890-Geobacillus thermodenitrificans-purified recombinant enzyme702817
972-Thermus thermophilus-mutant enzyme D138A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1011-Thermus thermophilus-mutant enzyme K65A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1016-Thermus thermophilus-mutant enzyme Q48A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1045-Thermus thermophilus-mutant enzyme R142E, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1046-Thermus thermophilus-mutant enzyme W69A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1065-Thermus thermophilus-mutant enzyme L39A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1076-Thermus thermophilus-mutant enzyme L124A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1092-Thermus thermophilus-mutant enzyme R142Y, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1194-Thermus thermophilus-mutant enzyme L18A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1214-Thermus thermophilus-mutant enzyme R142K, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1270-Thermus thermophilus-mutant enzyme R142Q, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1482-Thermus thermophilus-mutant enzyme R11A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1493-Thermus thermophilus-wild type enzyme, using L-ribulose as substrate, at pH 7.0 and 75°C713854
1619-Thermus thermophilus-wild type enzyme, using D-talose as substrate, at pH 7.0 and 75°C713854
1791-Thermus thermophilus-mutant enzyme R142A, using L-ribulose as substrate, at pH 7.0 and 75°C713854
2152-Thermus thermophilus-mutant enzyme R14N, using L-ribulose as substrate, at pH 7.0 and 75°C713854
additional information-Pseudomonas aeruginosa--2824
additional information-Candida albicans--2825
additional information-Homo sapiens--2826
additional information-Escherichia coli-mass spectrometry based method for the direct determination of kinetic konstants of enzyme661902
additional information-Bacillus subtilisQ9AGZ4substrate specificity, overview701797
additional information-Placopecten magellanicus-enzyme activity and metabolic parameters in different tissue at different reproductive stages in female and male animals, PMI shows no variability, overview705394

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6.57Amorphophallus konjac--2810
6.58Candida albicans, Homo sapiens, Saccharomyces cerevisiae, Sus scrofa--2828
77.2Saccharomyces cerevisiae--2624
7-Cassia coluteoides--2813
7-Xanthomonas campestris--2827
7-Geobacillus thermodenitrificans-assay at701812
7-Geobacillus thermodenitrificans--702817
7-Thermus thermophilus-maximal activity of the recombinant enzyme for L-ribulose isomerization713854
7-Thermus thermophilusQ5SIM4-714372
7.1-Escherichia coli, Saccharomyces cerevisiae-assay at702663
7.4-Pyrobaculum aerophilum--661679
7.5-Arabidopsis thaliana--693149
7.5-Bacillus subtilisQ9AGZ4recombinant enzyme701797
7.6-Placopecten magellanicus-assay at705394
7.6-Aspergillus fumigatusQ66WM4assay at705568
8-Sphingobium chungbukense--702869
8.5-Salmonella enterica subsp. enterica serovar TyphimuriumP25081-701472

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.59Amorphophallus konjac-about 50% of maximal activity at pH 5.5 and pH 9.02810
611Cassia coluteoides-pH 6.0: 50% of maximal activity, relative high activity up to pH 112813
6.38.8Pyrobaculum aerophilum-more than 50% of maximum activity in this range661679
6.58.5Bacillus subtilisQ9AGZ4-701797
6.58.5Geobacillus thermodenitrificans--702817
6.58.5Thermus thermophilusQ5SIM4-714372
6.59Salmonella enterica subsp. enterica serovar TyphimuriumP25081activity range701472

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
22-Salmonella enterica subsp. enterica serovar TyphimuriumP25081assay at room temperature701472
25-Escherichia coli, Saccharomyces cerevisiae-assay at702663
37-Sphingobium chungbukense-assay at702869
37-Aspergillus fumigatusQ66WM4assay at705568
40-Bacillus subtilisQ9AGZ4recombinant enzyme701797
52-Arabidopsis thaliana--693149
70-Geobacillus thermodenitrificans-assay at701812
70-Geobacillus thermodenitrificans--702817
75-Thermus thermophilus-maximal activity of the recombinant enzyme for L-ribulose isomerization713854
80-Thermus thermophilusQ5SIM4-714372
100-Pyrobaculum aerophilum--661679

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2050Bacillus subtilisQ9AGZ4-701797
6080Geobacillus thermodenitrificans--702817
7090Thermus thermophilusQ5SIM4-714372

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.9-Burkholderia cenocepacia-calculated690577
6-Burkholderia cepaciaQ06XM8calculated671785

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
arteryHomo sapiens--2624Manually annotated by BRENDA team
brainHomo sapiens--2826Manually annotated by BRENDA team
cell suspension cultureVigna angularis-growth on liquid and solid media, but no in presence of 90 mM mannose. After transfer of sucrose-grown cell onto medium containing mannose, cells grew little initially, but after a month lag period, they start to form callus colonies. Mannose-accomodated cells are capable of converting mannose to sucrose, with enhanced phosphomannose isomerase activity693863Manually annotated by BRENDA team
cormAmorphophallus konjac--2810Manually annotated by BRENDA team
digestive glandPlacopecten magellanicus--705394Manually annotated by BRENDA team
erythrocyteHomo sapiens, Sus scrofa--2624Manually annotated by BRENDA team
gonadPlacopecten magellanicus--705394Manually annotated by BRENDA team
heartHomo sapiens--2826Manually annotated by BRENDA team
intestinal mucosaBos taurus--2624Manually annotated by BRENDA team
muscleBos taurus, Cavia porcellus, Homo sapiens-skeletal2624Manually annotated by BRENDA team
muscleOryctolagus cuniculus--2624Manually annotated by BRENDA team
muscleOvis aries, Rattus norvegicus, Sus scrofa-skeletal2624Manually annotated by BRENDA team
musclePlacopecten magellanicus--705394Manually annotated by BRENDA team
pancreatic isletRattus norvegicus--2812Manually annotated by BRENDA team
placentaHomo sapiens--2826Manually annotated by BRENDA team
podCassia coluteoides, Cyamopsis tetragonoloba, Glycine max, Trigonella foenum-graecum--2813Manually annotated by BRENDA team
rootArabidopsis thalianaQ9M884-700488Manually annotated by BRENDA team
seedCassia coluteoides-developing and germinating2813Manually annotated by BRENDA team
seedlingArabidopsis thalianaQ9M884-700488Manually annotated by BRENDA team
testisBos taurus--2624Manually annotated by BRENDA team
leafArabidopsis thaliana-induction of expression under continuous light. Diurnal expression pattern in parallel with the total Pmi1 activity and the total ascorbic acid content in leaf693149Manually annotated by BRENDA team
additional informationArabidopsis thaliana-constitutive expression in both vegetative and reproductive organs; no expression in any organ under light. Under long term darkness, expression of isoform Pmi2 with concomitant decrease in ascorbic acid levels693149Manually annotated by BRENDA team
additional informationPlacopecten magellanicus-enzyme activity and metabolic parameters in different tissue at different reproductive stages in female and male animals, PMI shows no variability, overview705394Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
2gz6, downloadSCOP (2gz6)CATH (2gz6)Anabaena sp. CH1
1qwr, downloadSCOP (1qwr)CATH (1qwr)Bacillus subtilis (strain 168)
1pmi, downloadSCOP (1pmi)CATH (1pmi)Candida albicans (strain SC5314 / ATCC MYA-2876)
1tzb, downloadSCOP (1tzb)CATH (1tzb)Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
1tzc, downloadSCOP (1tzc)CATH (1tzc)Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
2wfp, downloadSCOP (2wfp)CATH (2wfp)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
3h1m, downloadSCOP (3h1m)CATH (3h1m)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
3h1w, downloadSCOP (3h1w)CATH (3h1w)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
3h1y, downloadSCOP (3h1y)CATH (3h1y)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
29000-Thermus thermophilus-gel filtration713854
29100-Thermus thermophilusQ5SIM4gel filtration714372
36000-Geobacillus thermodenitrificans-gel filtration, recombinant enzyme702817
36600-Bacillus subtilisQ9AGZ4gel filtration, recombinant enzyme701797
45000-Amorphophallus konjac-gel filtration2810
45000-Aeropyrum pernixQ9YE01gel filtration662220
46520-Homo sapiens-calculation from nucleotide sequence encoded by cDNA2826
46530-Homo sapiens-recombinant enzyme, electrospray mass spectroscopy2826
48000-Thermoplasma acidophilumQ9HIC2gel filtration662220
48740-Candida albicans-wild-type recombinant enzyme, electrospray mass spectroscopy2825
49060-Candida albicans-selenomethionine-labelled enzyme expressed in E. coli, electrospray mass spectroscopy2825
53000-Pyrococcus furiosus-SDS-PAGE694521
54000-Cyamopsis tetragonoloba-gel filtration2813
54000-Pseudomonas aeruginosa-bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase, gel filtration2824
58000-Xanthomonas campestris-gel filtration2827
59000-Glycine max-gel filtration2813
63000-Trigonella foenum-graecum-gel filtration2813
65000-Pyrobaculum aerophilum-sedimentation equilibrium, analytical ultracentrifugation661679
67000-Cassia coluteoides-enzyme from seeds, gel filtration2813
67000-Thermoplasma acidophilumQ9HIC2analytical ultracentrifugation662220
68000-Cassia coluteoides-enzyme from pods, gel filtration2813
74500-Cassia coluteoides-enzyme from pods and seeds, density gradient centrifugation2813

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Pseudomonas aeruginosa-x * 56000, SDS-PAGE2814
?Escherichia coli-x * 61000, calculation from nucleotide sequence2829
?Burkholderia cepaciaQ06XM8x * 55300, calculated, x * 55000, SDS-PAGE671785
?Burkholderia cenocepacia-x * 55716, calculated, x * 56000, SDS-PAGE690577
?Sphingobium chungbukense-x * 50000, recombinant His6-tagged enzyme, SDS-PAGE702869
dimerPyrobaculum aerophilum-2 * 36000, SDS-PAGE, 2 * 33548, calculated661679
dimerAeropyrum pernixQ9YE012 * 36000, SDS-PAGE, 2 * 36100, calculated662220
dimerThermoplasma acidophilumQ9HIC22 * 35000, SDS-PAGE, 2 * 35150, calculated662220
monomerPseudomonas aeruginosa-1 * 56000, bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase, SDS-PAGE2824
monomerXanthomonas campestris-1 * 58000, SDS-PAGE2827
monomerBacillus subtilisQ9AGZ4* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation701797
monomerGeobacillus thermodenitrificans-1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 36452, sequence calculation702817
monomerThermus thermophilus-1 * 29000, SDS-PAGE; 1 * 29054, calculated from amino acid sequence713854, 714372
additional informationPseudomonas aeruginosa-bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is composed of two independent enzymatic domains. The carboxyl terminus is critical for mannose-6-phosphate isomerase2823
additional informationSphingobium chungbukense-PMI possesses two domains with three conserved motifs: a GMP domain at the N-terminus and a PMI domain at the C-terminus702869

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Candida albicans-2820, 2822, 2825
homology modeling of structure and refinement by energy minimization and molecular dynamicsHomo sapiens-681498
-Pyrobaculum aerophilum-660585
both in complex with fructose 6-phosphate and with glucose 6-phosphatePyrobaculum aerophilumQ8ZWV0661100
both native form and in complex with 5-phosphoarabinonatePyrobaculum aerophilumQ8ZWV0662267
enzyme in apoform without metal ion, in the holoform with bound Zn2+, or complexed with bound inhibitor yttrium, or with Zn2+ and fructose 6-phosphate, microbatch method, 0.003 ml of protein solution and crystallization solution are mixed containing 4 mg/ml protein, 0.1 M magnesium acetate, 0.2 M sodium cacodylate, pH 6.5, 20% PEG 8000 and 5% dioxane, addition of 10 mM metal ions and 250 mM fructose 6-phosphate for complexed enzyme, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacementSalmonella enterica subsp. enterica serovar TyphimuriumP25081701472
to 1.66 A resolution, space group P212121. Preliminary structure solution by molecular replacement using the strucutre from Candida albicans mannose-6-phosphate isomeraseSalmonella enterica subsp. enterica serovar Typhimurium-690273

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
5.5-Amorphophallus konjac-40°C, 1 h, about 35% loss of activity2810
69.5Amorphophallus konjac-40°C, 1 h, no loss of activity2810
6.58Xanthomonas campestris-4°C, stable2827
10-Amorphophallus konjac-40°C, 1 h, about 25% loss of activity2810

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
25-Bacillus subtilisQ9AGZ4purified recombinant enzyme, half-life is 461 h701797
28-Xanthomonas campestris-half-life in absence of Zn2+: 110 min, half-life in presence of 0.0002 mM ZnCl2: 270 min2827
30-Bacillus subtilisQ9AGZ4purified recombinant enzyme, half-life is 325 h701797
35-Bacillus subtilisQ9AGZ4purified recombinant enzyme, half-life is 236 h701797
37-Saccharomyces cerevisiae-6 min, wild-type enzyme stable, mutant enzyme loses about 90% of activity2819
40-Amorphophallus konjac-pH 10, about 25% loss of activity; pH 5.5, 1 h, about 35% loss of activity; pH 6.0-9.5, 1 h, no loss of activity2810
40-Bacillus subtilisQ9AGZ4purified recombinant enzyme, half-life is 111 h701797
45-Amorphophallus konjac-pH 6.5, 30 min, native enzyme stable2809
45-Bacillus subtilisQ9AGZ4purified recombinant enzyme, half-life is 56 h701797
50-Bacillus subtilisQ9AGZ4purified recombinant enzyme, half-life is 10 h701797
55-Amorphophallus konjac-pH 6.5, 10 min, about 75% loss of native enzyme2809
60-Geobacillus thermodenitrificans-enzyme half-life is 388 h702817
6485Thermus thermophilusQ5SIM4the half-lives of the enzyme at 65, 70, 75, 80, and 85°C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively714372
6585Thermus thermophilus-the enzyme shows half-lives of 22, 10, 5.5, 2.1, and 0.3 h at 65, 70, 75, 80, and 85°C, respectively713854
65-Geobacillus thermodenitrificans-enzyme half-life is 73 h702817
70-Geobacillus thermodenitrificans-enzyme half-life is 27 h702817
100-Pyrobaculum aerophilum-melting temperature for thermal unfolding, 60 min, 50% residual activity661679
additional information-Bacillus subtilisQ9AGZ4first-order kinetics for thermal inactivation701797
additional information-Geobacillus thermodenitrificans-thermal inactivation of GTMpi follows first-order kinetics702817

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
EDTA-treated enzyme and 1,10-phenanthroline-treated enzyme is more susceptible to heat denaturation, addition of various metal ions causes the recovery of thermal stability. The most effective metal ion is Co2+, which causes the recovery of thermal stability to a level higher than that of the native enzymeAmorphophallus konjac-2809

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°C, unstableAmorphophallus konjac-2810

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Amorphophallus konjac-2810
recombinant enzyme 27fold from Escherichia coli strain ER2566 by affinity chromatographyBacillus subtilisQ9AGZ4701797
-Candida albicans-2828
normal and selenomethionine-labelled enzyme expressed in Escherichia coliCandida albicans-2825
recombinant enzyme 8.7fold from Escherichia coli strain ER2566Geobacillus thermodenitrificans-702817
-Homo sapiens-2826, 2828
HiTrap Ni-chelating column chromatography and Q-Sepharose column chromatographyHomo sapiens-716883
-Pseudomonas aeruginosa-2824
Ni-affinity columnPyrococcus furiosus-694521
-Saccharomyces cerevisiae-2828
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatographySalmonella enterica subsp. enterica serovar TyphimuriumP25081701472
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatographySphingobium chungbukense-702869
-Sus scrofa-2828
HisTrap HP column chromatographyThermus thermophilusQ5SIM4714372
-Xanthomonas campestris-2827

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Agrobacterium tumefaciensArabidopsis thalianaQ9M884700488
expression in Escherichia coliArabidopsis thaliana-693149
expression in Escherichia coli strain ER2566Bacillus subtilisQ9AGZ4701797
expression in Escherichia coliBurkholderia cenocepacia-690577
-Burkholderia cepaciaQ06XM8671785
wild-type and selenomethionine-labelled enzyme expressed in Escherichia coliCandida albicans-2825
-Escherichia coli-2829, 682354
Agrobacterium-based expression in Linum usitatissimumEscherichia coli-682360
expression in Brassica rapaEscherichia coli-681607, 682359
expression in Pseudomonas aeruginosaEscherichia coli-3354
use of enzyme as selectable markerEscherichia coli-682353
expression in Escherichia coli strain ER2566Geobacillus thermodenitrificans-702817
expression in Escherichia coli strain ER2566, coexpression with L-arabinose isomeraseGeobacillus thermodenitrificans-701812
cDNA under the control of the GAL1 promoter, expression in Saccharomyces cerevisiae and in Escherichia coliHomo sapiens-2826
expressed in Escherichia coli GI724 cellsHomo sapiens-716883
high level expression in Escherichia coli M15 as inclusion bodiesLeishmania mexicanaQ9GRS9652215
-Pseudomonas aeruginosa-2824
overexpressed under the control of the tac promoter in the broad-host-range controlled-expression vector pMMB22, expression in Escherichia coliPseudomonas aeruginosa-2814
overexpression in both mucoid and nonmucoid strains of Pseudomonas aeruginosaPseudomonas aeruginosa-3354
-Pyrobaculum aerophilum-661679
expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strainPyrococcus furiosus-694521
expression in Escherichia coliSalmonella enterica subsp. enterica serovar Typhimurium-690273
overexpression of the N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)Salmonella enterica subsp. enterica serovar TyphimuriumP25081701472
gene pmi, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)Sphingobium chungbukense-702869
-Streptomyces nodosus-693999
expressed in Escherichia coli BL21 cellsSulfolobus solfataricus-680450
expressed in Escherichia coli ER2566 cellsThermus thermophilus-713854, 714372

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
E410APseudomonas aeruginosa-about 25% of wild-type catalytic efficiency692361
E458APseudomonas aeruginosa-about 25% of wild-type catalytic efficiency692361
N433APseudomonas aeruginosa-about 25% of wild-type catalytic efficiency692361
R373APseudomonas aeruginosa-about 4% of wild-type catalytic efficiency692361
R408APseudomonas aeruginosa-complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity692361
R408KPseudomonas aeruginosa-complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity692361
R472APseudomonas aeruginosa-about 1% of wild-type catalytic efficiency692361
S309ASulfolobus solfataricus-42% decreased activity compared to the wild type enzyme680450
S309DSulfolobus solfataricus-96% decreased activity compared to the wild type enzyme680450
S309NSulfolobus solfataricus-73% decreased activity compared to the wild type enzyme680450
S309QSulfolobus solfataricus-78% decreased activity compared to the wild type enzyme680450
S309TSulfolobus solfataricus-64% decreased activity compared to the wild type enzyme680450
S309VSulfolobus solfataricus-64% decreased activity compared to the wild type enzyme680450
D138AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
D138AThermus thermophilusQ5SIM4the mutant shows 59% activity compared to the wild type enzyme714372
E132AThermus thermophilus-the mutants has no activity for L-ribulose713854
E132AThermus thermophilusQ5SIM4the mutant shows 1.9% activity compared to the wild type enzyme714372
E132DThermus thermophilusQ5SIM4the mutant shows 0.4% activity compared to the wild type enzyme714372
E132KThermus thermophilusQ5SIM4inactive714372
E132QThermus thermophilusQ5SIM4inactive714372
E132WThermus thermophilusQ5SIM4inactive714372
E67AThermus thermophilus-the mutants has no activity for L-ribulose713854
E67AThermus thermophilusQ5SIM4the mutant shows 2.5% activity compared to the wild type enzyme714372
E67DThermus thermophilusQ5SIM4the mutant shows 3.7% activity compared to the wild type enzyme714372
E67KThermus thermophilusQ5SIM4inactive714372
E67QThermus thermophilusQ5SIM4the mutant shows 0.8% activity compared to the wild type enzyme714372
E67WThermus thermophilusQ5SIM4inactive714372
H122AThermus thermophilus-the mutants has no activity for L-ribulose713854
H122AThermus thermophilusQ5SIM4the mutant shows 2.8% activity compared to the wild type enzyme714372
H122DThermus thermophilusQ5SIM4inactive714372
H122KThermus thermophilusQ5SIM4inactive714372
H122QThermus thermophilusQ5SIM4the mutant shows 2.0% activity compared to the wild type enzyme714372
H122WThermus thermophilusQ5SIM4inactive714372
H50AThermus thermophilus-the mutants has no activity for L-ribulose713854
H50AThermus thermophilusQ5SIM4the mutant shows 2.2% activity compared to the wild type enzyme714372
H50DThermus thermophilusQ5SIM4inactive714372
H50KThermus thermophilusQ5SIM4inactive714372
H50QThermus thermophilusQ5SIM4the mutant shows 2.0% activity compared to the wild type enzyme714372
H50WThermus thermophilusQ5SIM4inactive714372
K37AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
K37AThermus thermophilusQ5SIM4the mutant shows 21% activity compared to the wild type enzyme714372
K65AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
K65AThermus thermophilusQ5SIM4the mutant shows 15% activity compared to the wild type enzyme714372
L124AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
L18AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
L18AThermus thermophilusQ5SIM4the mutant shows 78% activity compared to the wild type enzyme714372
L39AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
L39AThermus thermophilusQ5SIM4the mutant shows 84% activity compared to the wild type enzyme714372
Q48AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
Q48AThermus thermophilusQ5SIM4the mutant shows 2.0% activity compared to the wild type enzyme714372
Q48DThermus thermophilusQ5SIM4inactive714372
Q48KThermus thermophilusQ5SIM4inactive714372
Q48NThermus thermophilusQ5SIM4inactive714372
Q48WThermus thermophilusQ5SIM4inactive714372
R11AThermus thermophilus-the enzyme shows about wild type specific activity for L-ribulose713854
R11AThermus thermophilusQ5SIM4the mutant shows 260% activity compared to the wild type enzyme714372
R142AThermus thermophilus-the enzyme shows increased specific activity for L-ribulose713854
R142AThermus thermophilusQ5SIM4the mutant shows 2.6% activity compared to the wild type enzyme714372
R142DThermus thermophilusQ5SIM4inactive714372
R142EThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
R142KThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
R142KThermus thermophilusQ5SIM4inactive714372
R142NThermus thermophilus-the specific activity and catalytic efficiency (kcat/Km) for L-ribulose using the R142N mutant are 1.4 and 1.6fold higher than those of the wild type enzyme, respectively713854
R142NThermus thermophilusQ5SIM4inactive714372
R142QThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
R142WThermus thermophilusQ5SIM4inactive714372
R142YThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
W13AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
W13AThermus thermophilusQ5SIM4the mutant shows 0.4% activity compared to the wild type enzyme714372
W13DThermus thermophilusQ5SIM4inactive714372
W13FThermus thermophilusQ5SIM4the mutant shows 41% activity compared to the wild type enzyme714372
W13HThermus thermophilusQ5SIM4the mutant shows 52% activity compared to the wild type enzyme714372
W13KThermus thermophilusQ5SIM4inactive714372
W13QThermus thermophilusQ5SIM4inactive714372
W13YThermus thermophilusQ5SIM4the mutant shows 68% activity compared to the wild type enzyme714372
W69AThermus thermophilus-the enzyme shows decreased specific activity for L-ribulose713854
W69AThermus thermophilusQ5SIM4the mutant shows 50% activity compared to the wild type enzyme714372
Y124AThermus thermophilusQ5SIM4the mutant shows 52% activity compared to the wild type enzyme714372
additional informationArabidopsis thaliana-knockout of isoform Pmi2 does not affect the total ascorbic acid levels in leaves; reduction of Pmi1 expression by RNA interference results in substantial decrease in the total ascorbic acid content of leaves693149
additional informationAspergillus fumigatusQ66WM4construction of a DELTApmi1 enzyme knockout mutant cell, that shows a significantly reduced growth rate at a high concentration of Man. Both inadequate and replete Man leads to an accumulation of intracellular Man-6-P and a reduction in the amount of alpha-glucan in the cell wall. Uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview705568
additional informationBrassica napus-transformation of Brassica napus with gene pmi as a selectable marker, transformation via Agrobacterium tumefaciens in hypocotyl explants, overview706204
additional informationBurkholderia cepaciaQ06XM8enzyme-deficient mutant is not impaired in synthesis of exopolysaccharide. However, the viscosity of aqueous solutions prepared with the exopolysaccharide produced by the mutant is significantly reduced compared with wild-type biopolymer and the mutant forms biofilms with a size reduced by 6fold671785
C150ACandida albicans-mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition2818
additional informationMus musculus-ablation of enzyme gene, homozygous embryos die around E11.5. Supplementation with D-mannose hastened their death. Embryos show growth retardation and placental hyperplasia. More than 90% of embryos failed to form yolk sac vasculature, and 35% failed chorioallantoic fusion662458
H411APseudomonas aeruginosa-about 25% of wild-type catalytic efficiency692361
additional informationPseudomonas aeruginosa-point mutation at nucleotide 961 greatly decreases enzyme activity2824
R479APseudomonas aeruginosa-about 3% of wild-type catalytic efficiency692361
additional informationSaccharomyces cerevisiae-thermolabile mutant enzyme2819
additional informationSaccharomyces cerevisiae-enzyme deleltion strain, cells are viable only if supplemented with extracellular mannose and glucose. Increase of extracellular mannose concentration results in significantly reduced growth rates without alterations in intracellular GDP-mannose levels and in increase of mannose 6-phosphate levels662318
additional informationStreptomyces nodosus-inactivation of the manA gene encoding phosphomannose isomerase results in production of amphotericins and their aglycones, 8-deoxyamphoteronolides. A double mutant lacking the phosphomannose isomerase and phosphomannomutase genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins693999

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisBacillus subtilisQ9AGZ4mannose-6-phosphate isomerase from Bacillus subtilis is applied for the production of L-ribose by direct isomerization of L-ribulose701797
analysisBrassica napus-development and optimization of a transformation method using the phosphomannose-isomerase gene pmi as a selectable marker for Brassica napus transformation via Agrobacterium tumefaciens, overview706204
pharmacologyCandida albicans-absence of mannose-6-phosphate isomerase causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs2822, 2825
agricultureEscherichia coli-non-antibiotic selection system based on heterologous expression of enzyme in Brassica rapa via Agrobacterium tumefaciens infection and screening for cotyledon explants that survive in media containing more than 5 g per l mannose. Presence of gene does not inhibit the growth of transgenic plants681607
agricultureEscherichia coli-expression system based on phosphomannose-isomerase gene as a selectable marker in Agrobacterium-based transformation and mannose as the selective agent for the transformation of apple. Selection of leaf explants on medium supplemented with mannose and sorbitol, integration of transgenes in the apple genome and their activity are confirmed682353
agricultureEscherichia coli-selection system for onion using Agrobacterium-based transformation with phosphomannose isomerase as selectable marker. Selection depends on detoxification of mannose 6-phosphate by conversion to fructose 6-phosphate in six-week-old embryonic calli. Transformation rates of 23-27% are obtained682354
agricultureEscherichia coli-use of enzyme as selectable marker in Agrobacterium-based expression of transgenes in Brassica rapa. Supplementation of media with 7 g per l mannose and 2% sucrose provides best conditions for the selection of transformed plants. Transformation rates of 1.4-3% are obtained682359
agricultureEscherichia coli-use of enzyme as selectable marker for Agrobacterium-medíated transformation of Linum usitatissimum. Transgenic flax plants able to root on mannose-containing medium are obtained on a combination of 20 g per l sucrose and 10 g per l mannose. Mean transformation efficacy is 3.6%682360
biotechnologyEscherichia coli-use of enzyme gene as selectable marker for transformation of Penniseum glaucum. Enzyme gene is a superior selectable marker for improving transformation efficiencies when compared to antibiotic or herbicide selectable marker genes663077
biotechnologyEscherichia coli-effective use of enzyme gene as selectable marker gene for transformation of embryogenic calli of Carica papaya663078
biotechnologyEscherichia coli-selection system for transformation of onion using enzyme gene and Agrobacterium. Transformation rates are around 25%663079
biotechnologyEscherichia coli-use of enzyme as selectable marker for transformation of Oriza sativa immature embryo via Agrobacterium663166
synthesisGeobacillus thermodenitrificans-L-ribose production of the enzyme in a coupled assay system with L-arabinose isomerase, EC 5.3.1.4, in recombinant Escherichia coli ER2566, AI/MPI ratio, 1:2.5, method optimization. L-Ribose is a potential starting material for the synthesis of many L-nucleoside-based pharmaceutical compounds701812
pharmacologyLeishmania mexicanaQ9GRS9the enzyme may be a target for anti-Leishmania drug development652215
biotechnologyOncidium Gower Ramsey-the pmi/mannose selection system is highly efficient for producing transgenic Oncidium Gower Ramsey without using antibiotics or herbicides716507
synthesisStreptomyces nodosus-inactivation of the manA gene encoding phosphomannose isomerase results in production of amphotericins and their aglycones, 8-deoxyamphoteronolides. A double mutant lacking the phosphomannose isomerase and phosphomannomutase genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins693999

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
6-phosphofructokinase deficiency[Exercise-induced muscular weakness, myalgia and contractures. I. A clinical review] PubMed
6-phosphofructokinase deficiency[Exercise-induced muscular weakness, myalgia and contractures. II. Casuistic contribution] PubMed
Alcohol Withdrawal DeliriumActivity of aldolase, aminotransferases, phosphohexoisomerase and ceruloplasmin in the course of delirium tremens. PubMed
Alcohol Withdrawal Delirium[Activity of aldolase, aminotransferases, phosphohexoisomerase and ceruloplasmin in the course of delirium tremens] PubMed
Anemia[Erythrocyte enzymes; activity of glycolytic enzymes of erythrocytes in anemia: phosphoglucomutase, phosphohexoisomerase, diphosphofructaldolase, lactic acid dehydrogenase.] PubMed
Biliary Tract Diseases[Serum iron and copper levels and serum activity of phosphohexoisomerase and glutamic-pyruvic transaminase in patients with liver and biliary tract disease] PubMed
Congenital Disorders of GlycosylationA zebrafish model of congenital disorders of glycosylation with phosphomannose isomerase deficiency reveals an early opportunity for corrective mannose supplementation. PubMed
Congenital Disorders of GlycosylationAffinity capture and elution/electrospray ionization mass spectrometry assay of phosphomannomutase and phosphomannose isomerase for the multiplex analysis of congenital disorders of glycosylation types Ia and Ib. PubMed
Congenital Disorders of GlycosylationCarbohydrate-deficient glycoprotein syndrome type 1 with profound thrombocytopenia and normal phosphomannomutase and phosphomannose isomerase activities. PubMed
Congenital Disorders of GlycosylationCarbohydrate-deficient glycoprotein syndrome type Ib. Phosphomannose isomerase deficiency and mannose therapy. PubMed
Congenital Disorders of GlycosylationExogenous mannose does not raise steady state mannose-6-phosphate pools of normal or N-glycosylation-deficient human fibroblasts. PubMed
Congenital Disorders of GlycosylationGenomic organization of the human phosphomannose isomerase (MPI) gene and mutation analysis in patients with congenital disorders of glycosylation type Ib (CDG-Ib). PubMed
Congenital Disorders of GlycosylationHyperinsulinemic hypoglycemia as a presenting sign in phosphomannose isomerase deficiency: A new manifestation of carbohydrate-deficient glycoprotein syndrome treatable with mannose. PubMed
Congenital Disorders of GlycosylationOntogeny of D-mannose transport and metabolism in rat small intestine. PubMed
Congenital Disorders of GlycosylationPhosphomannose isomerase deficiency: a carbohydrate-deficient glycoprotein syndrome with hepatic-intestinal presentation. PubMed
Congenital Disorders of GlycosylationSuccessful treatment of carbohydrate deficient glycoprotein syndrome type 1b with oral mannose. PubMed
Congenital Disorders of GlycosylationThe clinical spectrum of phosphomannose isomerase deficiency, with an evaluation of mannose treatment for CDG-Ib. PubMed
Congenital Disorders of Glycosylation[Carbohydrate-deficient glycoprotein syndrome (CDGS) type Ib. A hereditary metabolic disease and its therapy] PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesA zebrafish model of congenital disorders of glycosylation with phosphomannose isomerase deficiency reveals an early opportunity for corrective mannose supplementation. PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesAffinity capture and elution/electrospray ionization mass spectrometry assay of phosphomannomutase and phosphomannose isomerase for the multiplex analysis of congenital disorders of glycosylation types Ia and Ib. PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesExogenous mannose does not raise steady state mannose-6-phosphate pools of normal or N-glycosylation-deficient human fibroblasts. PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesGenetic and metabolic analysis of the first adult with congenital disorder of glycosylation type Ib: long-term outcome and effects of mannose supplementation. PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesGenomic organization of the human phosphomannose isomerase (MPI) gene and mutation analysis in patients with congenital disorders of glycosylation type Ib (CDG-Ib). PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesOntogeny of D-mannose transport and metabolism in rat small intestine. PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesPotent, selective, and orally available benzoisothiazolone phosphomannose isomerase inhibitors as probes for congenital disorder of glycosylation Ia. PubMed
Congenital, Hereditary, and Neonatal Diseases and AbnormalitiesThe clinical spectrum of phosphomannose isomerase deficiency, with an evaluation of mannose treatment for CDG-Ib. PubMed
Cystic FibrosisAlginate biosynthetic enzymes in mucoid and nonmucoid Pseudomonas aeruginosa: overproduction of phosphomannose isomerase, phosphomannomutase, and GDP-mannose pyrophosphorylase by overexpression of the phosphomannose isomerase (pmi) gene. PubMed
Cystic FibrosisFunctional analysis of the Burkholderia cenocepacia J2315 BceA(J) protein with phosphomannose isomerase and GDP-D: -mannose pyrophosphorylase activities. PubMed
DiphtheriaAssignment of hexosaminidase-B to chromosome 5, its segregation after diphtheria toxin selection, and the linkage of hexosaminidase-A, mannose phosphate isomerase, and pyruvate kinase (M2). PubMed,  PubMed
Ependymoma[Histochemical demonstration of glial enzyme activity. II. Reagent and neoplastic glia] PubMed
Fructose IntoleranceInhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerance. PubMed
Hepatitis[The diagnostic value of determining serum iron and copper levels and activity of phosphohexoisomerase and pyruvic-glutamic transaminase in viral hepatitis] PubMed
Hepatitis A[MICRODETERMINATION OF PHOSPHOHEXOISOMERASE (GLUCOSEPHOSPHATE ISOMERASE) IN THE SERUM AND THE CLINICAL IMPORTANCE OF ITS DETERMINATION IN INFECTIOUS HEPATITIS.] PubMed
HypoglycemiaHyperinsulinemic hypoglycemia as a presenting sign in phosphomannose isomerase deficiency: A new manifestation of carbohydrate-deficient glycoprotein syndrome treatable with mannose. PubMed
HypoglycemiaSevere hypoglycemia as a presenting symptom of carbohydrate-deficient glycoprotein syndrome. PubMed
LeishmaniasisBiochemical characterization of Leishmania (Viannia) braziliensis and Leishmania (Viannia) peruviana by isoenzyme electrophoresis. PubMed
LeishmaniasisUse of FTA cards for direct sampling of patients' lesions in the ecological study of cutaneous leishmaniasis. PubMed
Liver DiseasesSevere hypoglycemia as a presenting symptom of carbohydrate-deficient glycoprotein syndrome. PubMed
Liver Diseases[Studies on the serum enzymes in liver diseases; the activity of phosphohexoisomerase, aldolase and alkaline phosphatase.] PubMed
Liver FailureClinical approach to inherited metabolic disorders in neonates: an overview. PubMed
mannose-6-phosphate isomerase deficiencyA novel disorder of N-glycosylation due to phosphomannose isomerase deficiency. PubMed
mannose-6-phosphate isomerase deficiencyA zebrafish model of congenital disorders of glycosylation with phosphomannose isomerase deficiency reveals an early opportunity for corrective mannose supplementation. PubMed
mannose-6-phosphate isomerase deficiencyCarbohydrate-deficient glycoprotein syndrome type Ib. Phosphomannose isomerase deficiency and mannose therapy. PubMed
mannose-6-phosphate isomerase deficiencyClinical approach to inherited metabolic disorders in neonates: an overview. PubMed
mannose-6-phosphate isomerase deficiencyCongenital hepatic fibrosis in 3 siblings with phosphomannose isomerase deficiency. PubMed
mannose-6-phosphate isomerase deficiencyGenomic organization of the human phosphomannose isomerase (MPI) gene and mutation analysis in patients with congenital disorders of glycosylation type Ib (CDG-Ib). PubMed
mannose-6-phosphate isomerase deficiencyHyperinsulinemic hypoglycemia as a presenting sign in phosphomannose isomerase deficiency: A new manifestation of carbohydrate-deficient glycoprotein syndrome treatable with mannose. PubMed
mannose-6-phosphate isomerase deficiencyMannose inhibition as a significant marker for differentiating among novobiocin-resistant staphylococci of relevance in clinical microbiology. PubMed
mannose-6-phosphate isomerase deficiencyOral mannose therapy persistently corrects the severe clinical symptoms and biochemical abnormalities of phosphomannose isomerase deficiency. PubMed
mannose-6-phosphate isomerase deficiencyPhosphomannose isomerase deficiency as a cause of congenital hepatic fibrosis and protein-losing enteropathy. PubMed
mannose-6-phosphate isomerase deficiencyPhosphomannose isomerase deficiency: a carbohydrate-deficient glycoprotein syndrome with hepatic-intestinal presentation. PubMed
mannose-6-phosphate isomerase deficiencySevere hypoglycemia as a presenting symptom of carbohydrate-deficient glycoprotein syndrome. PubMed
mannose-6-phosphate isomerase deficiencyThe clinical spectrum of phosphomannose isomerase deficiency, with an evaluation of mannose treatment for CDG-Ib. PubMed
Muscular Diseases[Glycogen myopathy with a probable deficiency of phosphohexoisomerase. Preliminary report] PubMed
NeoplasmsAlterations in erythrocyte enzymes in cancer. PubMed
NeoplasmsEvaluation of Ehrlich's test as screening test for cancer. PubMed
NeoplasmsGlucosephosphate isomerase as a CSF marker for leptomeningeal metastasis. PubMed
Neoplasms[Clinical evaluation of the sedimentation reaction to cancer, indices of uropepsinogen and phosphohexoisomerase activity in the blood serum of patients with stomach cancer] PubMed
Neoplasms[Histochemical demonstration of glial enzyme activity. II. Reagent and neoplastic glia] PubMed
phosphorylase deficiency[Exercise-induced muscular weakness, myalgia and contractures. II. Casuistic contribution] PubMed
Pneumonia[Determination of phosphohexoisomerase activity in chronic pneumonia] PubMed
Protein-Losing EnteropathiesCongenital hepatic fibrosis in 3 siblings with phosphomannose isomerase deficiency. PubMed
Protein-Losing EnteropathiesPhosphomannose isomerase deficiency as a cause of congenital hepatic fibrosis and protein-losing enteropathy. PubMed
Protein-Losing EnteropathiesSeizures and stupor during intravenous mannose therapy in a patient with CDG syndrome type 1b (MPI-CDG). PubMed
Protein-Losing EnteropathiesSevere hypoglycemia as a presenting symptom of carbohydrate-deficient glycoprotein syndrome. PubMed
SarcomaSheep gene mapping: additional DNA markers included (CASB, CASK, LALBA, IGF-1 and AMH). PubMed
Stomach Neoplasms[Clinical evaluation of the sedimentation reaction to cancer, indices of uropepsinogen and phosphohexoisomerase activity in the blood serum of patients with stomach cancer] PubMed
Stomach Neoplasms[Effect of insulin on the activity of serum phosphohexoisomerase in gastric cancer] PubMed
ThrombocytopeniaCarbohydrate-deficient glycoprotein syndrome type 1 with profound thrombocytopenia and normal phosphomannomutase and phosphomannose isomerase activities. PubMed

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2624Noltmann, E.A.Aldose-ketose isomerasesThe Enzymes, 3rd Ed. (Boyer, P.D., ed.)6271-3541972Apis mellifera, Ascaris suum, Bos taurus, Cavia porcellus, Enterobacter aerogenes, Homo sapiens, Mammalia, Microorganisms, Nakazawaea holstii, Oryctolagus cuniculus, Ovis aries, Pseudomonas aeruginosa, Rattus norvegicus, Saccharomyces cerevisiae, Sus scrofa-
2806Gracy, R.W.; Noltmann, E.A.Studies on phosphomannose isomerase. II. Characterization as a zinc metalloenzymeJ. Biol. Chem.2434109-41161968Saccharomyces cerevisiae PubMed
2807Rose, I.A.; O'Connell, E.L.; Schray, K.J.Mannose 6-phosphate: anomeric form used by phosphomannose isomerase and its 1-epimerization by phosphoglucose isomeraseJ. Biol. Chem.2482232-22341973Saccharomyces cerevisiae PubMed
2809Murata, T.Studies on the phosphomannose isomerase of Amorphophallus konjac C. Koch II. Effect of divalent metal ions on the EDTA-treated enzymePlant Cell Physiol.16963-9701975Amorphophallus konjac-
2810Murata, T.Studies on the phosphomannose isomerase of Amorphophallus konjac C. Koch. I. Its isolation and some enzymic propertiesPlant Cell Physiol.16953-9611975Amorphophallus konjac-
2811Schray, K.J.; Waud, J.M.; Howell, E.E.Phosphomannose isomerase. Isomerization of the predicted beta-D-fructose 6-phosphateArch. Biochem. Biophys.189106-1081978Saccharomyces cerevisiae PubMed
2812Anjaneyulu, R.; Anjaneyulu, K.; Carpinelli, A.R.; Sener, A.; Malaisse, W.J.The stimulus-secretion coupling of glucose-induced insulin release: enzymes of mannose metabolism in pancreatic isletsArch. Biochem. Biophys.21254-621981Rattus norvegicus PubMed
2813Lee, B.T.; Matheson, N.K.Phosphomannoisomerase and phosphoglucoisomerase in seeds of Cassia coluteoides and some other legumes that synthesize galactomannanPhytochemistry23983-9871984Cassia coluteoides, Cyamopsis tetragonoloba, Glycine max, Trigonella foenum-graecum-
2814Gill, J.F.; Deretic, V.; Chakrabarty, A.M.Overproduction and assay of Pseudomonas aeruginosa phosphomannose isomeraseJ. Bacteriol.167611-6151986Pseudomonas aeruginosa PubMed
2816Wells, T.N.C.; Coulin, F.; Payton, M.A.; Proudfoot, A.E.I.Phosphomannose isomerase from Saccharomyces cerevisiae contains two inhibitory metal ion binding sitesBiochemistry321294-13011993Saccharomyces cerevisiae PubMed
2817Wells, T.N.C.; Payton, M.A.; Proudfoot, A.E.I.Inhibition of phosphomannose isomerase by mercury ionsBiochemistry337641-76461994Candida albicans, Homo sapiens, Saccharomyces cerevisiae, Sus scrofa PubMed
2818Wells, T.N.C.; Scully, P.; Paravicini, G.; Proudfoot, A.E.I.; Payton, M.A.Mechanism of irreversible inactivation of phosphomannose isomerase by silver ions and flamazineBiochemistry347896-79031995Candida albicans, Escherichia coli PubMed
2819Payton, M.A.; Rheinnecker, M.; Klig, L.S.; DeTiani, M.; Bowden, E.A novel Saccharomyces cerevisiae secretory mutant possesses a thermolabile phosphomannose isomeraseJ. Bacteriol.1732006-20101991Saccharomyces cerevisiae PubMed
2820Tolley, S.; Davies, G.; Hubbard, R.E.; Smith, D.J.; Proudfoot, A.E.I.; Payton, M.A.; Cleasby, A.; Wonacott, A.; Wells, T.N.C.Crystallization and preliminary X-ray analysis of Candida albicans phosphomannose isomeraseJ. Mol. Biol.237349-3501994Candida albicans PubMed
2821Jaeken, J.; Pirard, M.; Adamowicz, M.; Pronicka, E.; van Schaftingen, E.Inhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerancePediatr. Res.40764-7661996Homo sapiens PubMed
2822Cleasby, A.; Wonacott, A.; Skarzynski, T.; Hubbard, R.E.; Davies, G.J.; Proudfoot, A.E.I.; Bernard, A.R.; Payton, M.A.; Wells, T.N.C.The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 A resolutionNat. Struct. Biol.3470-4791996Candida albicans PubMed
2823May, T.B.; Shinabarger, D.; Boyd, A.; Chakrabarty, A.M.Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosaJ. Biol. Chem.2694872-48771994Pseudomonas aeruginosa PubMed
2824Shinabarger, D.; Berry, A.; May, T.B.; Rothmel, R.; Fialho, A.; Chakrabarty, A.M.Purification and characterization of phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosaJ. Biol. Chem.2662080-20881991Pseudomonas aeruginosa PubMed
2825Bernard, A.R.; Wells, T.N.C.; Cleasby, A.; Borlat, F.; Payton, M.A.; Proufoot, A.E.I.Selenomethionine labelling phosphomannose isomerase changes its kinetic propertiesEur. J. Biochem.230111-1181995Candida albicans PubMed
2826Proudfoot, A.E.I.; Turcatti, G.; Wells, T.N.C.; Payton, M.A.; Smith, D.J.Purification, cDNA cloning and heterologous expression of human phosphomannose isomeraseEur. J. Biochem.219415-4231994Homo sapiens PubMed
2827Papoutsopoulou, S.V.; Kyriakidis, D.A.Phosphomannose isomerase of Xanthomonas campestris: a zinc activated enzymeMol. Cell. Biochem.177183-1911997Xanthomonas campestris PubMed
2828Proudfoot, A.E.I.; Payton, M.A.; Wells, N.C.Purification and characterization of fungal and mammalian phosphomannose isomerasesJ. Protein Chem.13619-6271994Candida albicans, Homo sapiens, Saccharomyces cerevisiae, Sus scrofa PubMed
2829Froman, B.E.; Tait, R.C.; Gottlieb, L.D.Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coliMol. Gen. Genet.217126-1311989Escherichia coli PubMed
3354Sa-Correia, I.; Darzins, A.; Wang, S.K.; Berry, A.; Chakrabarty, A.M.Alginate biosynthetic enzymes in mucoid and nonmucoid Pseudomonas aeruginosa: overproduction of phosphomannose isomerase, phosphomannomutase, and GDP-mannose pyrophosphorylase by overexpression of the phosphomannose isomerase (pmi) geneJ. Bacteriol.1693224-32311987Escherichia coli, Pseudomonas aeruginosa PubMed
652215Garami, A.; Ilg, T.The role of phosphomannose isomerase in Leishmania mexicana glycoconjugate synthesis and virulenceJ. Biol. Chem.2766566-65752001Leishmania mexicana PubMed
652637Salvati, L.; Mattu, M.; Tiberi, F.; Polticelli, F.; Ascenzi, P.Inhibition of Saccharomyces cerevisiae phosphomannose isomerase by the NO-donor S-nitroso-acetyl-penicillamineJ. Enzyme Inhib.16287-2922001Saccharomyces cerevisiae PubMed
660585Swan, M.K.; Hansen, T.; Schonheit, P.; Davies, C.Crystallization and preliminary X-ray diffraction analysis of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilumActa Crystallogr. Sect. D601481-14832004Pyrobaculum aerophilum PubMed
660706Gao, H.; Yu, Y.; Leary, J.A.Mechanism and kinetics of metalloenzyme phosphomannose isomerase: measurement of dissociation constants and effect of zinc binding using ESI-FTICR mass spectrometryAnal. Chem.775596-56032005Escherichia coli PubMed
661100Swan, M.K.; Hansen, T.; Schonheit, P.; Davies, C.Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymesBiochemistry4314088-140952004Pyrobaculum aerophilum PubMed
661119Roux, C.; Lee, J.H.; Jeffery, C.J.; Salmon, L.Inhibition of type I and type II phosphomannose isomerases by the reaction intermediate analogue 5-phospho-D-arabinonohydroxamic acid supports a catalytic role for the metal cofactorBiochemistry432926-29342004Pseudomonas aeruginosa, Saccharomyces cerevisiae PubMed
661679Hansen, T.; Urbanke, C.; Schonheit, P.Bifunctional phosphoglucose/phosphomannose isomerase from the hyperthermophilic archaeon Pyrobaculum aerophilumExtremophiles8507-5122004Pyrobaculum aerophilum PubMed
661902Gao, H.; Chen, Y.; Leary, J.A.Kinetic measurements of phosphoglucose isomerase and phosphomannose isomerase by direct analysis of phosphorylated aldose-ketose isomers using tandem mass spectrometryInt. J. Mass Spectrom.240291-2992005Escherichia coli-
662220Hansen, T.; Wendorff, D.; Schonheit, P.Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamilyJ. Biol. Chem.2792262-22722004Aeropyrum pernix, Thermoplasma acidophilum PubMed
662267Swan, M.K.; Hansen, T.; Schonheit, P.; Davies, C.A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolutionJ. Biol. Chem.27939838-398452004Pyrobaculum aerophilum PubMed
662318Pitkanen, J.P.; Torma, A.; Alff, S.; Huopaniemi, L.; Mattila, P.; Renkonen, R.Excess mannose limits the growth of phosphomannose isomerase PMI40 deletion strain of Saccharomyces cerevisiaeJ. Biol. Chem.27955737-557432004Saccharomyces cerevisiae PubMed
662458Derossi, C.; Bode, L.; Eklund, E.A.; Zhang, F.; Davis, J.A.; Westphal, V.; Wang, L.; Borowsky, A.D.; Freeze, H.H.Ablation of mouse phosphomannose isomerase (Mpi) causes mannose-6-phosphate accumulation, toxicity, and embryonic lethalityJ. Biol. Chem.2815916-59272006Mus musculus PubMed
663077O'Kennedy, M.M.; Burger, J.T.; Botha, F.C.Pearl millet transformation system using the positive selectable marker gene phosphomannose isomerasePlant Cell Rep.22684-6902004Escherichia coli PubMed
663078Zhu, Y.J.; Agbayani, R.; McCafferty, H.; Albert, H.H.; Moore, P.H.Effective selection of transgenic papaya plants with the PMI/Man selection systemPlant Cell Rep.24426-4322005Escherichia coli PubMed
663079Aswath, C.R.; Mo, S.Y.; Kim, D.H.; Park, S.W.Agrobacterium and biolistic transformation of onion using non-antibiotic selection marker phosphomannose isomerasePlant Cell Rep.2592-992005Escherichia coli-
663166He, Z.; Fu, Y.; Si, H.; Hu, G.; Zhang, S.; Yu, Y.; Sun, Z.Phosphomannose-isomerase (pmi) gene as a selectable marker for rice transformation via AgrobacteriumPlant Sci.16617-222004Escherichia coli-
671785Sousa, S.A.; Moreira, L.M.; Wopperer, J.; Eberl, L.; Sa-Correia, I.; Leitao, J.H.The Burkholderia cepacia bceA gene encodes a protein with phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activitiesBiochem. Biophys. Res. Commun.353200-2062007Burkholderia cepacia PubMed
680450Ray, W.K.; Keith, S.M.; DeSantis, A.M.; Hunt, J.P.; Larson, T.J.; Helm, R.F.; Kennelly, P.J.A phosphohexomutase from the archaeon Sulfolobus solfataricus is covalently modified by phosphorylation on serineJ. Bacteriol.1874270-42752005Sulfolobus solfataricus PubMed
681498Xiao, J.; Guo, Z.; Guo, Y.; Chu, F.; Sun, P.Computational study of human phosphomannose isomerase: Insights from homology modeling and molecular dynamics simulation of enzyme bound substrateJ. Mol. Graph. Model.25289-2952006Homo sapiens PubMed
681607Ku, J.; Park, Y.; Park, Y.A non-antibiotic selection system uses the phosphomannose-isomerase (PMI) gene for Agrobacterium-mediated transformation of Chinese cabbageJ. Plant Biol.49115-1222006Escherichia coli-
682353Degenhardt, J.; Poppe, A.; Montag, J.; Szankowski, I.The use of the phosphomannose-isomerase/mannose selection system to recover transgenic apple plantsPlant Cell Rep.251149-11562006Escherichia coli PubMed
682354Aswath, C.R.; Mo, S.Y.; Kim, D.H.; Park, S.W.Agrobacterium and biolistic transformation of onion using non-antibiotic selection marker phosphomannose isomerase. [Erratum to document cited in CA145:001781]Plant Cell Rep.257472006Escherichia coli-
682359Min, B.W.; Cho, Y.N.; Song, M.J.; Noh, T.K.; Kim, B.K.; Chae, W.K.; Park, Y.S.; Choi, Y.D.; Harn, C.H.Successful genetic transformation of Chinese cabbage using phosphomannose isomerase as a selection markerPlant Cell Rep.26337-3442007Escherichia coli PubMed
682360Lamblin, F.; Aime, A.; Hano, C.; Roussy, I.; Domon, J.M.; Van Droogenbroeck, B.; Laine, E.The use of the phosphomannose isomerase gene as alternative selectable marker for Agrobacterium-mediated transformation of flax (Linum usitatissimum)Plant Cell Rep.26765-7722007Escherichia coli PubMed
690273Gowda, G.; Sagurthi, S.R.; Savithri, H.S.; Murthy, M.R.Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the mannose 6-phosphate isomerase from Salmonella typhimuriumActa Crystallogr. Sect. F6481-842008Salmonella enterica subsp. enterica serovar Typhimurium PubMed
690577Sousa, S.A.; Moreira, L.M.; Leitao, J.H.Functional analysis of the Burkholderia cenocepacia J2315 BceAJ protein with phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activitiesAppl. Microbiol. Biotechnol.801015-10222008Burkholderia cenocepacia PubMed
692361Lee, H.J.; Chang, H.Y.; Venkatesan, N.; Peng, H.L.Identification of amino acid residues important for the phosphomannose isomerase activity of PslB in Pseudomonas aeruginosa PAO1FEBS Lett.5823479-34832008Pseudomonas aeruginosa PubMed
693149Maruta, T.; Yonemitsu, M.; Yabuta, Y.; Tamoi, M.; Ishikawa, T.; Shigeoka, S.Arabidopsis phosphomannose isomerase 1, but not phosphomannose isomerase 2, is essential for ascorbic acid biosynthesisJ. Biol. Chem.28328842-288512008Arabidopsis thaliana PubMed
693863Kato, A.; Inouhe, M.Mannose accommodation of Vigna angularis cells on solid agar medium involves its possible conversion to sucrose mediated by enhanced phosphomannose isomerase activityJ. Plant Res.121339-3492008Vigna angularis PubMed
693999Nic Lochlainn, L.; Caffrey, P.Phosphomannose isomerase and phosphomannomutase gene disruptions in Streptomyces nodosus: impact on amphotericin biosynthesis and implications for glycosylation engineeringMetab. Eng.1140-472009Streptomyces nodosus PubMed
694521Mizanur, R.M.; Pohl, N.L.B.Phosphomannose isomerase/GDP-mannose pyrophosphorylase from Pyrococcus furiosus: a thermostable biocatalyst for the synthesis of guanidinediphosphate-activated and mannose-containing sugar nucleotidesOrg. Biomol. Chem.72135-21392009Pyrococcus furiosus PubMed
700488Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis rootsNew Phytol.184457-4722009Arabidopsis thaliana PubMed
701472Sagurthi, S.R.; Gowda, G.; Savithri, H.S.; Murthy, M.R.Structures of mannose-6-phosphate isomerase from Salmonella typhimurium bound to metal atoms and substrate: implications for catalytic mechanismActa Crystallogr. Sect. D65724-7322009Salmonella enterica subsp. enterica serovar Typhimurium PubMed
701797Yeom, S.J.; Ji, J.H.; Kim, N.H.; Park, C.S.; Oh, D.K.Substrate specificity of a mannose-6-phosphate isomerase from Bacillus subtilis and its application in the production of L-riboseAppl. Environ. Microbiol.754705-47102009Bacillus subtilis PubMed
701812Yeom, S.J.; Kim, N.H.; Park, C.S.; Oh, D.K.L-ribose production from L-arabinose by using purified L-arabinose isomerase and mannose-6-phosphate isomerase from Geobacillus thermodenitrificansAppl. Environ. Microbiol.756941-69432009Geobacillus thermodenitrificans PubMed
701879Li, H.; Xu, H.; Xu, H.; Li, S.; Ouyang, P.K.Biosynthetic pathway of sugar nucleotides essential for welan gum production in Alcaligenes sp. CGMCC2428Appl. Microbiol. Biotechnol.86295-3032010Alcaligenes sp. PubMed
702663Foret, J.; de Courcy, B.; Gresh, N.; Piquemal, J.P.; Salmon, L.Synthesis and evaluation of non-hydrolyzable D-mannose 6-phosphate surrogates reveal 6-deoxy-6-dicarboxymethyl-D-mannose as a new strong inhibitor of phosphomannose isomerasesBioorg. Med. Chem.177100-71072009Escherichia coli, Saccharomyces cerevisiae PubMed
702817Yeom, S.J.; Kim, N.H.; Yoon, R.Y.; Kwon, H.J.; Park, C.S.; Oh, D.K.Characterization of a mannose-6-phosphate isomerase from Geobacillus thermodenitrificans that converts monosaccharidesBiotechnol. Lett.311273-12782009Geobacillus thermodenitrificans PubMed
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LINKS TO OTHER DATABASES (specific for EC-Number 5.3.1.8)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)